298 results on '"Plants analysis"'
Search Results
2. Evaluation of near-infrared spectroscopy for analysis of soil and plant in agriculture
- Author
-
Kim, Nicholas D. and Kim, Nicholas D.
- Abstract
In this research, a critical scientific appraisal of Near Infrared (NIR) spectroscopy for the analysis of soil and plant is presented. Near Infrared measurements in the study were collected using a KESNIR spectrometer with a scanning range of 400-1700 nm and a large scanning area. NIR was shown as the instrument of choice because of its versatility, nondestruction of sample on analysis and rapid measurement times. The focus of this study was to derive and test correlations between NIR spectra of soil and plant samples and concentrations of nutrient-related variables in these samples (as measured using conventional techniques). These NIR correlations effectively constitute a series of calibrations. The concentrations of a number of elements ( or other soil or plant physicochemical properties) will then be able to be reliably estimated on the basis of a sample's NIR spectrum alone. Part of this project is devoted to deriving calibrations, and the rest will focus on assessing how well these NIR calibrations perform, by comparison ofNIRpredicted values to those obtained using conventional chemical extraction followed by analyte-specific instrumental analysis. In order to achieve the above for soil testing, calibrations included samples from all 15 New Zealand soil orders and subsoil types, geographical regions, and land use. Most of the soil and plant samples analysed have been taken from the pool of such samples routinely submitted to AgResearch for analysis. In addition, to date, no studies have been reported in which NIR spectra have been recorded for a full range of soil orders in a country. In the case of the NIR measurements, field-moist soil and plant samples could be used, rather than dried and ground samples. This represents a considerable saving of time and effort. One aim of this project was to investigate and validate measurements for soil and plant samples by NIR using field-moist samples. This would then enable the measurement of nutrient status in the fie
- Published
- 2006
3. Chloroplast biogenesis. Detection of monovinyl protochlorophyll(ide) b in plants.
- Author
-
Shedbalkar VP, Ioannides IM, and Rebeiz CA
- Subjects
- Esters analysis, Magnetic Resonance Spectroscopy, Molecular Structure, Plants analysis, Plants metabolism, Protochlorophyllide analysis, Protochlorophyllide chemistry, Protochlorophyllide metabolism, Chlorophyll metabolism, Chloroplasts metabolism, Protochlorophyllide analogs & derivatives
- Abstract
The occurrence of protochlorophyllide b and protochlorophyllide b phytyl ester in green plants is described. The chemical structure of protochlorophyllide b phytyl ester was established by proton nuclear magnetic resonance, fast atom bombardment mass spectroscopic analysis, and chemical derivatization coupled to electronic spectroscopic analysis. The macrocycles of protochlorophyll(ide) b are identical to those of conventional protochlorophyll(ide) except for the presence of a formyl group instead of a methyl group at position 3 of the macrocycles. They differ from chlorophyll(ide) b by the presence of an oxidized double bond at positions 7 and 8 of the macrocycles. The trivial name protochlorophyll(ide) b is proposed to differentiate these two tetrapyrroles from conventional protochlorophyll(ide), which in turn will be referred to as protochlorophyll(ide) a. Protochlorophyll(ide) b appears to be widely distributed in green plants. Its molar extinction coefficients in 80% acetone and diethyl ether are reported. The impact of this discovery on the heterogeneity of the chlorophyll a and b biosynthetic pathways is discussed.
- Published
- 1991
4. Purification and amino acid sequence of a bitter gourd inhibitor against an acidic amino acid-specific endopeptidase of Streptomyces griseus.
- Author
-
Ogata F, Miyata T, Fujii N, Yoshida N, Noda K, Makisumi S, and Ito A
- Subjects
- Amino Acid Sequence, Amino Acids analysis, Glutamates metabolism, Glutamic Acid, Molecular Sequence Data, Peptides metabolism, Protease Inhibitors metabolism, Seeds analysis, Sequence Alignment, Substrate Specificity, Peptides isolation & purification, Plants analysis, Protease Inhibitors isolation & purification, Serine Endopeptidases metabolism, Streptomyces griseus enzymology
- Abstract
An inhibitor (BGIA) against an acidic amino acid-specific endopeptidase of Streptomyces griseus (Glu S. griseus protease) was isolated from seeds of the bitter gourd Momordica charantia L., and its amino acid sequence was determined. The molecular weight of BGIA based on the amino acid sequence was calculated to be 7419. BGIA competitively inhibited Glu S. griseus protease with an inhibition constant (Ki) of 70 nM, and gel filtration analyses suggested that BGIA forms a 1:1 complex with this protease. However, two other acidic amino acid-specific endopeptidases, protease V8 from Staphylococcus aureus and Bacillus subtilis proteinase (Glu B. subtilis protease), were not inhibited by BGIA. BGIA had no inhibitory activity against chymotrypsin, trypsin, porcine pancreatic elastase, and papain, although subtilisin Carlsberg was strongly inhibited. The amino acid sequence of BGIA shows similarity to potato chymotrypsin inhibitor, barley subtilisin-chymotrypsin inhibitor CI-1 and CI-2, and leech eglin C, especially around the reactive site. Although the residue at the putative reactive site of these inhibitors is leucine or methionine, the corresponding amino acid in BGIA is alanine.
- Published
- 1991
5. Extreme variations in the ratios of non-synonymous to synonymous nucleotide substitution rates in signal peptide evolution.
- Author
-
Garcia-Maroto F, Castagnaro A, Sanchez de la Hoz P, Maraña C, Carbonero P, and García-Olmedo F
- Subjects
- Amino Acid Sequence, Amylases chemistry, Amylases genetics, Base Sequence, Biological Evolution, Hordeum analysis, Hordeum genetics, Molecular Sequence Data, Plant Proteins chemistry, Plant Proteins genetics, Plants analysis, Plastocyanin chemistry, Plastocyanin genetics, Protein Precursors chemistry, Protein Sorting Signals chemistry, Sequence Homology, Nucleic Acid, Triticum analysis, Triticum genetics, Trypsin Inhibitors chemistry, alpha-Amylases antagonists & inhibitors, Amylases antagonists & inhibitors, Plants genetics, Protein Precursors genetics, Protein Sorting Signals genetics, Sweetening Agents, Trypsin Inhibitors genetics
- Abstract
Nucleotide sequences encoding signal peptides from the precursors of alpha-amylase/trypsin inhibitors from cereals are homologous to those corresponding to the precursors of thaumatin II and of plastocyanins. Non-synonymous (KA) and synonymous (KS) rates of nucleotide substitutions have been calculated for all possible binary combinations. Extreme variation in KA/KS ratios has been observed; from the 0.167 average found within the plastocyanin family to an average of 1.90 calculated for the inhibitors/thaumatin II transition. A similar calculation has been carried out for the signal peptide sequences of thionins, which are unrelated to those of the alpha-amylase/trypsin inhibitor family, and an average KA/KS of 0.12 has been obtained. This variation can be largely explained in terms of an empirical index of stability related to amino acid composition and seems to be independent of functional constraints.
- Published
- 1991
- Full Text
- View/download PDF
6. Inhibition of HIV-reverse transcriptase activity by some phloroglucinol derivatives.
- Author
-
Nakane H, Arisawa M, Fujita A, Koshimura S, and Ono K
- Subjects
- Base Sequence, DNA, Molecular Sequence Data, Molecular Structure, Phloroglucinol metabolism, Phloroglucinol pharmacology, Plants analysis, HIV enzymology, Phloroglucinol analogs & derivatives, Reverse Transcriptase Inhibitors
- Abstract
Four phloroglucinol derivatives, named mallotophenone (5-methylene-bis-2,6-dihydroxy-3-methyl-4-methoxyacetophenone), mallotochromene (8-acetyl-5,7-dihydroxy-6-(3-acetyl-2,4- dihydroxy-5-methyl-6-methoxybenzyl)-2,2-dimethylchromene), mallotojaponin (3-(3,3(dimethylallyl)5-(3(acetyl-2,4- dihydroxy-5-methyl-6-methoxybenzyl)-phloracetophenone) and mallotolerin (3-(3-methyl-2-hydroxybut-3-enyl)-5(3-acetyl-2,4- dihydroxy-5-methyl-6-methoxybenzyl)-phloracetophenone), have been tested for their ability to inhibit the activity of human immunodeficiency virus (HIV)-reverse transcriptase. Under the reaction conditions with (rA)n.(dT)12-18 as the template.primer, the enzyme activity was inhibited by approximately 70% in the presence of 10 micrograms/ml mallotochromene or mallotojaponin, whereas mallotophenone and mallotolerin were much less inhibitory to the enzyme. The enzyme activity was also inhibited, though to lesser extent, by these compounds under similar conditions with initiated MS-2 phage RNA as the template.primer. The mode of inhibition was, as analyzed with mallotojaponin, competivite with respect to the template.primer, (rA)n.(dT)12-18, and non-competitive with respect to the triphosphate substrate, dTTP. The Ki value of mallotojaponin for HIV-reverse transcriptase was determined to be 6.1 microM.
- Published
- 1991
- Full Text
- View/download PDF
7. R-phycoerythrin as a fluorescent label for immunolocalization of bound atrazine residues.
- Author
-
Sohn G and Sautter C
- Subjects
- Atrazine analysis, Fluorescent Antibody Technique, Fluorescent Dyes, Phycoerythrin, Plants analysis
- Abstract
We established a highly sensitive immunofluorescence procedure for localizing bound atrazine in the aquatic macrophytes Elodea canadensis and E. densa. The technique included biotin-labeled anti-rabbit IgG as a first enhancement step and R-phycoerythrin (R-PE) coupled to streptavidin for fluorescent labeling as a second improvement on the procedure. A comparison with the conventional indirect immunofluorescence method confirmed the superior results of the R-PE approach. The use of atrazine-free plants (grown in charcoal-filtered water) and a variety of other controls excluded both contaminating atrazine and nonspecific incubation constituents as sources of tissue staining. Pre-incubations to block nonspecific binding sites proved to be unnecessary in this system. The highly sensitive procedure described here might be a useful tool for the localization of tissue-bound pesticides in general and possibly of other haptens as well.
- Published
- 1991
- Full Text
- View/download PDF
8. Gap junction protein homologue from Arabidopsis thaliana: evidence for connexins in plants.
- Author
-
Meiners S, Xu A, and Schindler M
- Subjects
- Amino Acid Sequence, Base Sequence, Connexins, DNA genetics, DNA isolation & purification, Immunoblotting, Membrane Proteins chemistry, Membrane Proteins genetics, Molecular Sequence Data, Plants genetics, Membrane Proteins analysis, Plants analysis
- Abstract
An Arabidopsis thaliana library constructed in the pBluescript expression vector lambda ZAP II (Stratagene) was screened with three affinity-purified antibodies raised against (i) rat liver connexin 32, (ii) a polypeptide from soybean root cells that migrates with a molecular mass of 29 kDa in SDS/polyacrylamide gels and is immunologically related to rat liver connexin, and (iii) a synthetic peptide corresponding to a sequence in rat liver connexin 32. A single clone was obtained whose gene product demonstrated immunological crossreactivity with all three reagents. The cDNA from this clone contained 1171 base pairs and coded for a protein of 280 amino acids with a calculated molecular mass of 32,339 Da (migrates as a 29-kDa polypeptide in SDS/polyacrylamide gels). The sequence homology observed between the 32-kDa polypeptide of Arabidopsis and connexin 32 from rat liver, in conjunction with observed similarities in predicted number and distribution of hydrophobic domains, sites for posttranslational modification, and basic pI, provides strong evidence that the biological range for connexin-type proteins may now be considered to include the plant kingdom.
- Published
- 1991
- Full Text
- View/download PDF
9. Proton nuclear magnetic resonance investigation of adrenodoxin. Assignment of aromatic resonances and evidence for a conformational similarity with ferredoxin from Spirulina platensis.
- Author
-
Miura S and Ichikawa Y
- Subjects
- Amino Acid Sequence, Animals, Cattle, Magnetic Resonance Spectroscopy, Molecular Conformation, Molecular Sequence Data, Swine, Adrenodoxin chemistry, Ferredoxins chemistry, Plants analysis
- Abstract
Bovine, porcine and sheep adrenodoxin, and the trypsin-resistant form of bovine adrenodoxin have been studied by one- and two-dimensional 1H-NMR spectroscopy. Assignment of the resonances for all the aromatic amino acids with resolved aromatic resonances have been made by correlating NMR spectra with the amino acid sequences from various species. Slowly exchanging amide protons and downfield shifted alpha-protons of His10 and Phe11 suggest possible involvement in beta-sheet structure. The effects on the assigned resonances due to the specific spin-label with a nitroxide radical at Cys95 have been analyzed on a two-dimensional 1H-NMR spectrum. The present results provide evidence for a structural similarity with a model for the structure of adrenodoxin based on a sequence alignment with that of Spirulina platensis ferredoxin, for which X-ray crystallographic data is available. epsilon-Methyl groups of Met120 and Met122 have been assigned by comparing 1H-NMR spectra of adrenodoxin with those of the trypsin-resistant form of adrenodoxin which is specifically cleaved at Arg115. epsilon-Methyl groups of Met120 and Met122 have an exceptionally long longitudinal relaxation time compared with those of valyl and leucyl methyl groups, suggesting that the COOH-terminal peptide spanning over 13 amino acids rotates rather freely in the solvent.
- Published
- 1991
- Full Text
- View/download PDF
10. Detection and identification of loline and its analogues in horse urine.
- Author
-
Takeda A, Suzuki E, Kamei K, and Nakata H
- Subjects
- Animals, Gas Chromatography-Mass Spectrometry, Plants analysis, Spectrophotometry, Infrared, Alkaloids urine, Horses urine
- Abstract
Several kinds of loline-type alkaloids, norloline, loline, N-acetylnorloline, N-acetylloline, N-formylnorloline, N-formylloline and N-methylloline were detected in the urine of race-horses. Furthermore, a new compound of the alkaloids, N-senecioylnorloline, was also found and identified. These compounds were mainly identified by means of gas chromatography-mass spectrometry (GC-MS) and gas chromatography-fourier transform-infrared spectrometry (GC-FT-IR). A certain plant of Gramineae containing four kinds of loline-type alkaloids was found in a bale of hay used for the horse forage. The taxonomic feature of the plant was different from known plants containing loline-type alkaloids. The common fragmentation of loline-type alkaloids under electron ionization was briefly discussed.
- Published
- 1991
- Full Text
- View/download PDF
11. Two new components of 9 and 14 kDa from spinach photosystem I complex.
- Author
-
Ikeuchi M and Inoue Y
- Subjects
- Amino Acid Sequence, Light-Harvesting Protein Complexes, Molecular Sequence Data, Molecular Weight, Photosystem I Protein Complex, Photosynthetic Reaction Center Complex Proteins chemistry, Plants analysis
- Abstract
Two formerly-uncharacterized subunits of 9 kDa and 14 kDa were found in spinach PSI complex. The 9 kDa subunit was released upon removal of antenna chlorophyll complex, whereas the 14 kDa subunit was tightly bound to the core complex. We determined the N-terminal amino acid sequence of the 9 kDa, and an internal sequence of the 14 kDa subunit after protease treatment, since the N-terminus of the latter protein was blocked. These partial sequences suggested that both subunits are new PSI components.
- Published
- 1991
- Full Text
- View/download PDF
12. [The importance of bioindicators in the evaluation of radioactive contamination].
- Author
-
Marović G
- Subjects
- Animals, Plants analysis, Tissue Distribution, Cesium Radioisotopes analysis, Radioactive Fallout analysis, Strontium Radioisotopes analysis
- Abstract
The paper is a survey of investigations into radioactive contamination of selected plant and animal species (bioindicators) which have the capacity for multiple accumulation of fission products. Literature data on the contamination of bioindicators are compared with special reference to the accumulation of 131I, 137Cs and 90Sr as a result of atmospheric nuclear experiments and the nuclear accident at Chernobyl.
- Published
- 1990
13. Benzene: environmental partitioning and human exposure.
- Author
-
Hattemer-Frey HA, Travis CC, and Land ML
- Subjects
- Air analysis, Animals, Biodegradation, Environmental, Cattle, Fishes, Humans, Meat analysis, Milk chemistry, Plants analysis, Smoking adverse effects, Soil analysis, United States, Water analysis, Benzene analysis, Environmental Exposure
- Abstract
A multimedia transport model was used to evaluate the environmental partitioning of benzene. Measured and predicted environmental concentrations were used to estimate the accumulation of benzene in the food chain and the subsequent extent of human exposure from inhalation and ingestion. Results show that benzene partitions mainly into air (99.9%) and that inhalation is the dominant pathway of human exposure, accounting for more than 99% of the total daily intake of benzene. Ingestion of contaminated food items represents only a minor pathway of human exposure. The long-term average daily intake of benzene by the general population of the U.S. was estimated using three independent methods. Intake estimates based on measured personal air exposures, measured exhaled air concentrations, and a pharmacokinetically derived adipose tissue concentration (73, 63, and 72 micrograms/day, respectively) are in good agreement. Although inhalation is the primary route of human exposure to background levels of benzene in the environment, smoking was found to be the largest anthropogenic source of background human exposure to benzene.
- Published
- 1990
- Full Text
- View/download PDF
14. An inhibitor of protein synthesis initiation from Alhagi kirgisorum S.
- Author
-
Smailov SK, Mukhamedzhanov BG, Lee AV, Iskakov BK, and Denisenko ON
- Subjects
- Animals, Eukaryotic Initiation Factor-2 metabolism, Guanosine Triphosphate metabolism, In Vitro Techniques, Plants analysis, RNA, Transfer, Met metabolism, Rabbits, Reticulocytes, Ribosomes metabolism, Peptide Chain Initiation, Translational drug effects, Phenols pharmacology
- Abstract
Polyproanthocyanidin--a plant phenolic compound from Alhagi kirgisorum S. effectively inhibited protein synthesis in rabbit reticulocyte and wheat germ cell-free systems. Poly-proanthocyanidin inhibited translation only at the level of initiation and not at the elongation level and aminoacylation of tRNA. The inhibitory effect of the phenolic compound is due to the blockage of the ternary complex formation of eIF-2 with GTP and initiator Met-tRNA.
- Published
- 1990
- Full Text
- View/download PDF
15. Complete amino acid sequence of luffin-a, a ribosome-inactivating protein from the seeds of sponge gourd (Luffa cylindrica).
- Author
-
Islam MR, Nishida H, and Funatsu G
- Subjects
- Amino Acid Sequence, Amino Acids analysis, Carbohydrates analysis, Chromatography, Gel, Chromatography, High Pressure Liquid, Chymotrypsin, Cyanogen Bromide, Molecular Sequence Data, Peptides analysis, Peptides isolation & purification, Ribosome Inactivating Proteins, Type 1, Ribosomes drug effects, Succinates analysis, Succinates chemical synthesis, Trypsin, Plant Proteins chemistry, Plants analysis
- Abstract
The complete amino acid sequence of luffin-a has been determined. Twenty-two peptides were isolated from the tryptic digest of luffin-a and sequenced employing the DABITC/PITC double coupling method. Overlaping of these peptides was achieved by analyzing the chymotryptic peptides or CNBr-fragments of luffin-a and their S. aureus V8 protease peptides. Luffin-a consists of 248 amino acid residues and its relative molecular mass is calculated to be 27,021 Da, excluding the attached sugar chains reasoned to be present at each Asn residue of positions 28, 33, 77, 84, 206, and 227. A comparison with the sequence of ricin A-chain showed 33% sequence identity indicating that these proteins are homologous.
- Published
- 1990
16. Plant constituents biologically active to insects. VI. Antifeedants for larvae of the yellow butterfly, Eurema hecabe mandarina, in Osmunda japonica. (2).
- Author
-
Numata A, Takahashi C, Fujiki R, Kitano E, Kitajima A, and Takemura T
- Subjects
- Animals, Larva, Feeding Behavior drug effects, Insecticides pharmacology, Lepidoptera physiology, Plants analysis
- Abstract
Three antifeedants for larvae of the yellow butterfly, Eurema hecabe mandarina de l'Orza, were isolated from Osmunda japonica Thunb. and identified as osmundalin, parasorboside and methyl (3S,5S)-5-hydroxy-3-(beta-D-glucopyranosyloxy)hexanoate. In the course of isolation of the antifeedants, a new glycoside, dihydroisoosmudalin (9), was isolated together with maltol beta-D-glucopyranoside, 2-deoxy-L-ribopyranolactone, 5-hydroxymethyl.2-furfural and glycerin. The structure of 9 was elucidated as (4R,5S)-5-(beta-D-glucopyranosyloxy)hexan-4-olide on the basis of chemical and spectroscopic evidence.
- Published
- 1990
- Full Text
- View/download PDF
17. Characterization of matteuccin, the 2.2S storage protein of the ostrich fern. Evolutionary relationship to angiosperm seed storage proteins.
- Author
-
Rödin J and Rask L
- Subjects
- 2S Albumins, Plant, Amino Acid Sequence, Biological Evolution, Cross Reactions, Molecular Sequence Data, Molecular Weight, Peptides immunology, Peptides isolation & purification, Plants analysis, Precipitin Tests, Seeds analysis, Plant Proteins immunology, Plant Proteins isolation & purification
- Abstract
The 2.2S spore storage protein (matteuccin) of the ostrich fern, Matteuccia struthiopteris, has been isolated and characterized. It is a small basic protein consisting of two disulfide-linked polypeptides with approximate molecular masses of 3.0 kDa and 8.0 kDa. At least four different isoforms exist where two of the forms differ from the other by having a slightly smaller heavy chain. Amino acid analysis reveals that the 2.2S protein is rich in arginine. Almost complete amino acid sequence information was obtained for the light chain and a partial sequence for the heavy chain. Amino acid sequence comparison reveals that this protein shows a high similarity to seed storage proteins in different angiosperm species in spite of the fact that the common ancestor of ferns and angiosperms lived more than 300 million years ago.
- Published
- 1990
- Full Text
- View/download PDF
18. The 55-kDa polypeptide released from spinach thylakoid membranes with 1 M LiCl is not the beta subunit of chloroplast F1.
- Author
-
Sato MH, Hisabori T, and Yoshida M
- Subjects
- Amino Acid Sequence, Chloroplasts analysis, Chloroplasts enzymology, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Intracellular Membranes enzymology, Macromolecular Substances, Membrane Proteins metabolism, Molecular Sequence Data, Molecular Weight, Plants analysis, Plants enzymology, Ribulose-Bisphosphate Carboxylase genetics, Sequence Homology, Nucleic Acid, Intracellular Membranes analysis, Membrane Proteins isolation & purification, Plant Proteins isolation & purification, Proton-Translocating ATPases isolation & purification, Ribulose-Bisphosphate Carboxylase isolation & purification
- Abstract
It was reported by Frasch et al. (Frasch, W. D., Green, J., Caguiat, J., and Mejia, A. (1989) J. Biol. Chem. 264, 5064-5069) that washing spinach thylakoid membranes with 1 M LiCl caused the release of the beta subunit of chloroplast F1 (CF1) which, existing as 180-kDa complexes of beta 3, retained considerable ATPase activity. We repeated their procedures and confirmed that a CF1 beta-like 55-kDa polypeptide was a major constituent of the 1 M LiCl-washed extract. However, the extract contained another polypeptide of which the Mr was 14,000, and these two polypeptides comprised a complex with approximate Mr 550,000 that had the same mobility in native polyacrylamide gel electrophoresis as that of ribulose-1,5-bisphosphate carboxylase. Only very low ATPase activity, less than 1% of the reported value, was detected for the extract and the purified complex. Antibody against the beta subunit of F1 from a thermophilic bacterium PS3 showed a clear cross-reactivity with the CF1 beta subunit but not with the 55-kDa polypeptide. Analysis of the N-terminal amino acid sequences of the 55- and 14-kDa polypeptides and the whole complex revealed that the complex was ribulose-1,5-bisphosphate carboxylase and that the 55- and 14-kDa polypeptides were its large and small subunits, respectively.
- Published
- 1990
19. Structure of the cyclohexapeptide cleromyrine II trihydrate.
- Author
-
Declercq JP, Tinant B, Bashwira S, and Hootelé C
- Subjects
- Amino Acid Sequence, Crystallization, Magnetic Resonance Spectroscopy, Mass Spectrometry, Molecular Sequence Data, Molecular Structure, X-Ray Diffraction, Peptides, Cyclic isolation & purification, Plants analysis
- Abstract
C29H40N6O7.3H2O, Mr = 638.7, trigonal, P3(1)21, a = 14.190 (2), c = 29.833 (4) A, V = 5202 (1) A3, Z = 6, Dx = 1.22 g cm-3, Cu K alpha, lambda = 1.54178 A, mu = 7.8 cm-1, F(000) = 2052, T = 291 K, R = 0.069 for 1942 observed reflections. The new cyclohexapeptide cleromyrine II was isolated from Clerodendrum myricoides. Its structure was established by spectroscopic and X-ray diffraction methods as cyclo(-Gly-Tyr-Gly-Pro-Leu-Pro-). The conformation essentially consists of two beta-turns including the Pro residues and one central very short antiparallel beta-sheet stabilized by two intramolecular hydrogen bonds: N(Tyr2)...O(Leu5) = 2.94 (2) A and N(Leu5)...O(Tyr2) = 3.02 (2) A.
- Published
- 1990
- Full Text
- View/download PDF
20. Accumulation, stability, and localization of a major chloroplast heat-shock protein.
- Author
-
Chen Q, Lauzon LM, DeRocher AE, and Vierling E
- Subjects
- Antibodies immunology, Chloroplasts analysis, Electrophoresis, Polyacrylamide Gel, Fabaceae, Heat-Shock Proteins genetics, Heat-Shock Proteins immunology, Heat-Shock Proteins physiology, Immunoblotting, Plants analysis, Plants, Medicinal, RNA, Messenger genetics, RNA, Messenger metabolism, Temperature, Chloroplasts metabolism, Heat-Shock Proteins metabolism
- Abstract
Diverse higher plant species synthesize low molecular weight (LMW) heat shock proteins (HSPs) which localize to chloroplasts. These proteins are homologous to LMW HSPs found in the cytoplasm of all eukaryotes, a class of HSPs whose molecular mode of action is not understood. To obtain basic information concerning the role of chloroplast HSPs, we examined the accumulation, stability, tissue specificity, and intra-chloroplast localization of HSP21, the major LMW chloroplast HSP in pea. Intact pea plants were subjected to heat stress conditions which would be encountered in the natural environment and HSP21 mRNA and protein levels were measured in leaves and roots. HSP21 was not detected in leaves or roots before stress, but the mature, 21-kD protein accumulated in direct proportion to temperature and HSP21 mRNA levels in both tissues. All of the HSP21 in leaves was localized to chloroplasts; there was no evidence for its transport into other organelles. In chloroplast fractionation experiments, greater than 80% of HSP21 was recovered in the soluble chloroplast protein fraction. The half-life of HSP21 at control temperatures was 52 +/- 12 h, suggesting the protein's function is critical during recovery as well as during stress. We hypothesize that HSP21 functions in a catalytic fashion in both photosynthetic and nonphotosynthetic plastids.
- Published
- 1990
- Full Text
- View/download PDF
21. Polypeptide composition of higher plant photosystem I complex. Identification of psaI, psaJ and psaK gene products.
- Author
-
Ikeuchi M, Hirano A, Hiyama T, and Inoue Y
- Subjects
- Amino Acid Sequence, Electrophoresis, Polyacrylamide Gel, Fabaceae analysis, Light-Harvesting Protein Complexes, Molecular Sequence Data, Molecular Weight, Photosynthetic Reaction Center Complex Proteins, Photosystem I Protein Complex, Plants analysis, Plants, Medicinal, Sequence Homology, Nucleic Acid, Chlorophyll isolation & purification, Plant Proteins isolation & purification
- Abstract
High resolution gel electrophoresis of the native photosystem I complex retaining light-harvesting chlorophyll complex revealed the presence of three low-molecular-mass proteins of 7, 4.1 and 3.9 kDa in spinach, and 6.8, 4.4 and 4.1 kDa in pea, in addition to the other well-characterized higher-molecular-mass components. Upon further detergent treatment to deplete light-harvesting chlorophyll complex, the 7 kDa and 4.1 kDa proteins were removed from the photosystem I core complex of spinach, while the 3.9 kDa protein was retained. N-terminal sequencing demonstrated that the 4.1 kDa proteins from both spinach and pea correspond to the gene product of ORF42/44 in chloroplast genome of liverwort and higher plants, which was previously hypothesized as a photosystem I gene (psaJ) based on sequence homology with the cyanobacterial photosystem I component of 4.1 kDa [(1989) FEBS Lett. 253, 257-263]. N-terminal sequence of the spinach 3.9 kDa and pea 4.4 kDa proteins fitted with chloroplast ORF36/40 (psaI) although no homologue has been found in cyanobacteria. The spinach 7 kDa and pea 6.8 kDa proteins correspond to the nuclear-encoded psaK product and significantly matched with the N-terminal sequence of the cyanobacterial 6.5 kDa subunit. The evolutional conservation of the psaJ and psaK seems to suggest their intrinsic role(s) in photosystem I.
- Published
- 1990
- Full Text
- View/download PDF
22. Simultaneous multielement analysis of diet samples by inductively coupled plasma mass spectrometry and inductively coupled plasma atomic emission spectrometry.
- Author
-
Shiraishi K, McInroy JF, and Igarashi Y
- Subjects
- Adult, Animals, Cattle, Humans, Liver analysis, Male, Mass Spectrometry methods, Plants analysis, Spectrophotometry, Atomic methods, Diet, Minerals blood
- Abstract
Diet samples were collected by a duplicated portion study for an adult male in both Mito, Japan and Los Alamos, U.S.A. The ashed samples were analyzed with inductively coupled plasma mass spectrometry (ICP-MS) and inductively coupled atomic emission spectrometry (ICP-AES) for 22 elements. The trace and ultratrace elements, Ba, Mo, Ni, Co, Cd, Cs, Tl, Pb, Bi, Th, and U were determined by ICP-MS. The major and minor elements, Na, K, P, Ca, Mg, Fe, Zn, Mn, Al, Sr, and Cu were determined by ICP-AES. Accuracy and precision for some elements were examined by analyzing National Institute of Standards and Technology (formerly National Bureau of Standards) Standard Reference Materials, 1577b Bovine Liver, and 1573 Tomato Leaves. Simultaneous multielement analyses of diet samples by using the two methods were found to be very useful.
- Published
- 1990
- Full Text
- View/download PDF
23. The early nodulin transcript ENOD2 is located in the nodule parenchyma (inner cortex) of pea and soybean root nodules.
- Author
-
van de Wiel C, Scheres B, Franssen H, van Lierop MJ, van Lammeren A, van Kammen A, and Bisseling T
- Subjects
- Amino Acid Sequence, Base Sequence, DNA genetics, DNA isolation & purification, Fabaceae, Molecular Sequence Data, Nucleic Acid Hybridization, Plant Development, Plant Proteins analysis, Plants genetics, Plants, Medicinal, RNA genetics, RNA Probes, RNA, Antisense, Glycine max, Tissue Distribution, Membrane Proteins, Plant Proteins genetics, Plants analysis, RNA analysis, Transcription, Genetic
- Abstract
A pea cDNA clone homologous to the soybean early nodulin clone pGmENOD2 that most probably encodes a cell wall protein was isolated. The derived amino acid sequence of the pea ENOD2 protein shows that it contains the same repeating pentapeptides, ProProHisGluLys and ProProGluTyrGln, as the soybean ENOD2 protein. By in situ hybridization the expression of the ENOD2 gene was shown to occur only in the inner cortex of the indeterminate pea nodule. The transcription of the pea ENOD2 gene starts when the inner cortical cells develop from the nodule meristem. In the determinate soybean nodule the ENOD2 gene is expressed in the inner cortex as well as in cells surrounding the vascular bundle that connects the nodule with the root central cylinder. The term 'nodule inner cortex' is misleading, as there is no direct homology with the root inner cortex. Therefore, we propose to consider this tissue as nodule parenchyma. A possible role of ENOD2 in a major function of the nodule parenchyma, namely creating an oxygen barrier for the central tissue with the Rhizobium containing cells, is discussed.
- Published
- 1990
- Full Text
- View/download PDF
24. Isolation and characterization of the proteinase inhibitor-inducing factor from tomato leaves. Identity and activity of poly- and oligogalacturonide fragments.
- Author
-
Bishop PD, Pearce G, Bryant JE, and Ryan CA
- Subjects
- Carbohydrates analysis, Chromatography, DEAE-Cellulose, Chromatography, Gel, Chromatography, High Pressure Liquid, Oligosaccharides analysis, Hexuronic Acids, Pectins isolation & purification, Plants analysis, Uronic Acids analysis
- Abstract
Mild acid hydrolysis of a small (Mr = 6 kDa) pectic polysaccharide isolated from tomato leaves, an inducer of the synthesis and accumulation of two proteinase inhibitors in excised tomato plants, yielded a alpha-D-polygalacturonic acid polymer with degree of polymerization = 20 that retained proteinase inhibitor-inducing activity. Enzymic and acid hydrolysis of this polygalacturonan yielded a series of alpha-1,4-D-galacturonic acid oligomers with degrees of polymerization from 2 to 6 which were purified to homogeneity and assayed for proteinase inhibitor-inducing activity in young excised tomato plants. All of the oligomers exhibited activity. The hexagalacturonide possessed the highest activity and the trimer the lowest. The evidence supports a possible role for plant cell wall fragments as systemic messengers that regulate the expression of proteinase inhibitor genes in plant leaves in response to pest attacks.
- Published
- 1984
25. Purification and characterization of tomato polygalacturonase converter.
- Author
-
Pressey R
- Subjects
- Chemical Phenomena, Chemistry, Chromatography methods, Chromatography, Gel, Hot Temperature, Hydrogen-Ion Concentration, Molecular Weight, Papain, Plants enzymology, Polygalacturonase isolation & purification, Polygalacturonase metabolism, Pronase, Trypsin, Plant Proteins isolation & purification, Plants analysis
- Abstract
Extracts of ripe tomatoes contain two forms of polygalacturonase (PG I and PG II). A heat-stable component that binds PG II to produce PG I has been isolated from tomato fruit. This component has been named polygalacturonase converter (PG converter). The PG converter has been purified by gel filtration, ion-exchange chromatography and chromatofocusing. It appears to be a protein with a relative molecular mass of 102000. It was readily inactivated by papain and pronase. The converter was labile at alkaline conditions, and treatment of PG I at pH 11 released free PG II. A similar factor with a lower molecular mass was extracted from tomato foliage.
- Published
- 1984
- Full Text
- View/download PDF
26. Could mosses be used for the subsequent mapping of the Chernobyl fallout?
- Author
-
Daróczy S, Bolyós A, Dezsö Z, Pázsit A, Nagy J, and Nagy M
- Subjects
- Cesium Radioisotopes analysis, Humans, Ukraine, Accidents, Nuclear Reactors, Plants analysis, Radioactive Fallout
- Published
- 1988
- Full Text
- View/download PDF
27. Immunological evidence for structural similarity among lectins from species of the Solanaceae.
- Author
-
Kilpatrick DC, Jeffree CE, Lockhart CM, and Yeoman MM
- Subjects
- Acetylglucosamine pharmacology, Fluorescent Antibody Technique, Immunodiffusion, Oligosaccharides pharmacology, Plant Lectins, Plants analysis, Lectins immunology
- Published
- 1980
- Full Text
- View/download PDF
28. On the hypotensive substances in plants. (1) Method for extraction and effects on blood pressure in rats [proceedings].
- Author
-
Okamoto K, Suzuki T, Miyake H, Murakami T, Iizuka Y, Honda S, and Kakehi K
- Subjects
- Animals, Cerebrovascular Disorders prevention & control, Hypertension prevention & control, Plant Extracts therapeutic use, Rats, Blood Pressure drug effects, Plants analysis
- Published
- 1979
- Full Text
- View/download PDF
29. Electrophoretic purification of chlorophyll a/b-protein complexes from Chlamydomonas reinhardtii and spinach and analysis of their polypeptide compositions.
- Author
-
Delepelaire P and Chua NH
- Subjects
- Light-Harvesting Protein Complexes, Macromolecular Substances, Molecular Weight, Peptides isolation & purification, Photosynthetic Reaction Center Complex Proteins, Species Specificity, Spectrophotometry, Chlamydomonas analysis, Chlorophyll isolation & purification, Cytochromes isolation & purification, Plant Proteins isolation & purification, Plants analysis
- Published
- 1981
30. Cyclopentenoid cyanohydrin glycosides with unusual sugar residues.
- Author
-
Olafsdottir ES, Cornett C, and Jaroszewski JW
- Subjects
- Hydrolysis, Magnetic Resonance Spectroscopy, Molecular Conformation, Carbohydrates chemistry, Cyclopentanes chemistry, Glycosides chemistry, Plants analysis
- Abstract
The cyclopentenoid cyanohydrin glycosides passicapsin and passibiflorin have been identified as (1S, 4R)-1-(beta-D-glucopyranosyloxy)-4-(2,6-dideoxy-beta-D-xylo-hex o pyranosyloxy)-2-cyclopentene-1-carbonitrile and (1S, 4R)-1-(beta-D-glucopyranosyloxy)-4-(6-deoxy-beta-D-gulopyranosy loxy)-2- cyclopentene-1-carbonitrile, respectively, using one- and two-dimensional NMR spectroscopy, selective acid-catalysed cleavage of the glycosidic linkages of the deoxy sugars, and optical rotation data.
- Published
- 1989
- Full Text
- View/download PDF
31. The nucleotide sequence of spinach chloroplast methionine elongator tRNA.
- Author
-
Pirtle R, Calagan J, Pirtle I, Kashdan M, Vreman H, and Dudock B
- Subjects
- Base Sequence, Escherichia coli analysis, Nucleic Acid Conformation, Nucleic Acid Hybridization, Plants analysis, Species Specificity, Chloroplasts analysis, RNA, Transfer, Amino Acyl
- Abstract
The nucleotide sequence of spinach chloroplast methionine elongator tRNA (sp. chl. tRNAm Met) has been determined. This tRNA is considerably more homologous to E. coli tRNAm Met (67% homology) than to the three known eukaryotic tRNAm Met (50-55% homology). Sp. chl. tRNAm Met, like the eight other chloroplast tRNAs sequenced, contains a methylated GG sequence in the dihydrouridine loop and lacks unusual structural features which have been found in several mitochondrial tRNAs.
- Published
- 1981
- Full Text
- View/download PDF
32. Chloride binding to photosystem II in the dark is in slow exchange.
- Author
-
Shachar-Hill Y, Beck WF, and Brudvig GW
- Subjects
- Chlorides analysis, Darkness, Electron Spin Resonance Spectroscopy, Energy Transfer, Light-Harvesting Protein Complexes, Magnetic Resonance Spectroscopy, Oxygen analysis, Photosynthetic Reaction Center Complex Proteins, Photosystem II Protein Complex, Protein Binding, Chlorides metabolism, Chlorophyll analysis, Photosynthesis, Plant Proteins analysis, Plants analysis
- Abstract
We have studied the 35Cl- NMR line broadening in the presence of photosystem II (PS II) membranes from spinach in the dark. In the presence of NH3 (which other work has shown to competitively inhibit chloride binding to PS II) we observed no decrease in 35 Cl- linewidths. We conclude that binding of Cl- to the O2 evolving center in PS II in the dark (previously demonstrated by EPR) is in slow exchange on the NMR timescale. We assign the observed line broadening to interaction with non-specific binding sites and with free paramagnetics.
- Published
- 1989
- Full Text
- View/download PDF
33. Reversible redistribution of phytochrome within the cell upon conversion to its physiologically active form.
- Author
-
Mackenzie JM Jr, Coleman RA, Briggs WR, and Pratt LH
- Subjects
- Cytoplasm analysis, Immunologic Techniques, Light, Peroxidases, Photochemistry, Plants ultrastructure, Pigments, Biological analysis, Plant Proteins analysis, Plants analysis
- Abstract
The intracellular localization of phytochrome was seen in dark-grown oat (Avena sativa L., cv. Garry) and rice (Oryza sativa L., cv. unknown) shoots after various light treatments using an indirect peroxidase-antiperoxidase antibody labeling method. Phytochrome is generally distributed throughout the cytoplasm in cells of tissue that had not been exposed to light prior to fixation. Within, at most, 8 min after the onset of saturating red irradiation, phytochrome, now present in the far-red-absorbing form, becomes associated with discrete regions of the cell. These regions do not appear to be nuclei, plastids, or mitochondria. After phototransformation back to the red-absorbing form originally present, phytochrome slowly resumes its general distribution. It is possible that this discrete localization of the far-red-absorbing form of phytochrome represents a physiologically significant binding with a receptor site in the cell.
- Published
- 1975
- Full Text
- View/download PDF
34. Isolation and chromatographic behaviour of phenylalanine tRNA from barley embryos.
- Author
-
Labuda D, Janowicz Z, Haertlé T, and Augustyniak J
- Subjects
- Amino Acyl-tRNA Synthetases metabolism, Chromatography, DEAE-Cellulose, Chromatography, Gel, Chromatography, Ion Exchange, Hordeum analysis, Phenylalanine, Plants metabolism, Saccharomyces cerevisiae enzymology, Spectrometry, Fluorescence, Plants analysis, RNA, Transfer isolation & purification, RNA, Transfer metabolism
- Abstract
Two fractions of phenylalanine tRNA (tRNA(Phe) (1) and tRNA(Phe) (2)) were purified by BD-cellulose and RPC-5 chromatography of crude tRNA isolated from barley embryos. Successive RPC-5 rechromatography runs of tRNA(Phe) (2) showed its conversion into more stable tRNA(Phe) (1), suggesting that the two fractions have essentially the same primary structure. Both tRNA(Phe) (1) and tRNA(Phe) (2) had about the same acceptor activity, but tRNA(Phe) (2) was aminoacylated much faster than tRNA(Phe) (1). RPC-5 chromatography of crude aminoacylated tRNA showed higher contents of phe-tRNA(Phe) (2) than of phe-tRNA(Phe) (1) but the ratio of these two fractions estimated by relative fluorescence intensity was about 1. Fluorescence spectra of tRNA(Phe) from barley embryos suggest that it contains Y base similar to Y(w) from wheat tRNA(Phe).
- Published
- 1974
- Full Text
- View/download PDF
35. 1,25-Dihydroxycholecalciferol-like activity in Solanum malacoxylon: purification and partial characterization.
- Author
-
Peterlik M and Wasserman RH
- Subjects
- Animals, Biological Assay, Calcium metabolism, Chickens, Chromatography, Duodenum drug effects, Duodenum metabolism, Intestinal Mucosa drug effects, Intestinal Mucosa metabolism, Rickets metabolism, Silicon Dioxide, Dihydroxycholecalciferols isolation & purification, Dihydroxycholecalciferols pharmacology, Hydroxycholecalciferols, Plants analysis
- Published
- 1975
- Full Text
- View/download PDF
36. Characterization of envelope membrane polypeptides from spinach chloroplasts.
- Author
-
Joyard J, Grossman A, Bartlett SG, Douce R, and Chua NH
- Subjects
- Electrophoresis, Polyacrylamide Gel, Immunodiffusion, Molecular Weight, Plants analysis, Chloroplasts analysis, Intracellular Membranes analysis, Membrane Proteins analysis, Peptides analysis
- Published
- 1982
37. Plants with potential to enhance significant tumor growth.
- Author
-
Caldwell ME and Brewer WR
- Subjects
- Animals, Cell Division drug effects, Drug Evaluation, Preclinical, Organ Size drug effects, Plants analysis, Species Specificity, Carcinogens, Neoplasms, Experimental physiopathology, Plant Extracts toxicity
- Abstract
Of 20,000 plant extracts submitted to the National Cancer Institute antitumor screens from 1960 to 1980, over 95% exhibited inadequate tumor-inhibiting activity or promoted tumor growth. Of these, 50 extracts representing 42 species showed significant levels of tumor growth enhancement compared to controls on the basis of tumor weights when the extracts were administered to test and control animals dosed equally on the basis of implanted tumor weights. Because of the continuing threat of environmentally induced or promoted cancer in the human population, the species identified in this report are deemed worthy of studies designed to quantitate the risks of contact by botanists, hikers, plant hobbyists, and field workers. Even more fundamental, studies of these plants could provide knowledge of new compounds under the influence of which tumor growth is enhanced. Further studies might also reveal the mechanisms of this tumor enhancement.
- Published
- 1983
38. Rubber elongation factor from Hevea brasiliensis. Identification, characterization, and role in rubber biosynthesis.
- Author
-
Dennis MS and Light DR
- Subjects
- Antigens, Plant, Chromatography, Chromatography, High Pressure Liquid, Detergents pharmacology, Immunoglobulin G, Immunologic Techniques, Latex analysis, Microscopy, Electron, Molecular Weight, Organophosphorus Compounds metabolism, Trees, Trypsin pharmacology, Allergens, Dimethylallyltranstransferase metabolism, Hemiterpenes, Latex metabolism, Plant Proteins, Plants analysis, Proteins analysis, Rubber metabolism, Transferases metabolism
- Abstract
The presence of a protein, rubber elongation factor (REF), which is tightly bound to serum-free rubber particles purified from Hevea brasiliensis latex, is necessary for prenyltransferases from a number of sources to add multiple cis-isoprene units to rubber molecules. These prenyltransferases show normal farnesyl pyrophosphate synthase activity (two trans additions of isopentenyl pyrophosphate to dimethylallyl pyrophosphate) in the absence of REF bound to rubber particles. REF bound to rubber molecules can be highly purified from all other proteins in whole latex by treatment of rubber particles with low concentrations of detergent. Treatment of rubber particles with trypsin which hydrolyzes bound REF, removal of REF with high concentrations of various detergents, or treatment of whole latex with polyclonal antibodies specific for REF all prevent prenyltransferase from adding [14C]isopentenyl pyrophosphate to rubber molecules. However, we have not been successful using detergent-solubilized REF in the reconstitution of in vitro rubber biosynthesis with either REF-depleted rubber particles or allylic pyrophosphate primers. REF has a molecular mass of 14,600 Da and is associated specifically with rubber particles in whole latex. It makes up between 10-60% of the total protein in whole latex but is absent in C-serum, the supernatant fluid obtained when rubber particles are removed by centrifugation. The amount of REF in whole latex is proportional to the rubber content. Based on a number average molecular mass of 500,000 Da for rubber and the content of rubber and REF in whole latex or serum-free rubber particles, the stoichiometry of REF molecules to rubber molecules is 1:1 in both cases. There is sufficient REF to form a monomolecular protein layer coating large rubber particles (700-1,000 nm). In the electron microscope, serum-free rubber particle preparations contain particles with diameters from 800 to as small as 10 nm. In the presence of 1% sodium dodecyl sulfate no particles smaller than 100 nm are observed. We suggest that the smaller particles may be mainly composed of REF molecules.
- Published
- 1989
39. Plant essential oils--candidate treatments for atheroma? [proceedings].
- Author
-
Bell GD, Burgess A, Ellis WR, Middleton A, Middleton B, Orchard TJ, and White DA
- Subjects
- Female, Humans, Male, Plants analysis, Arteriosclerosis drug therapy, Oils, Volatile therapeutic use
- Published
- 1980
- Full Text
- View/download PDF
40. Structures of two natural hypotensive Diels-Alder type adducts, mulberrofurans F and G, from the cultivated mulberry tree (Morus lhou KOIDZ.).
- Author
-
Fukai T, Hano Y, Hirakura K, Nomura T, Uzawa J, and Fukushima K
- Subjects
- Animals, Antihypertensive Agents pharmacology, Benzofurans pharmacology, Chemical Phenomena, Chemistry, Rabbits, Terpenes pharmacology, Antihypertensive Agents isolation & purification, Benzofurans isolation & purification, Plants analysis, Terpenes isolation & purification
- Published
- 1985
- Full Text
- View/download PDF
41. Several properties of the partially purified proteinase inhibitor in eggplant exocarp.
- Author
-
Kanamori M, Ibuki F, Yamada M, Tashiro M, and Miyoshi M
- Subjects
- Chymotrypsin antagonists & inhibitors, Enzyme Inhibitors isolation & purification, Enzyme Inhibitors pharmacology, Plants analysis, Pronase antagonists & inhibitors, Structure-Activity Relationship, Subtilisins antagonists & inhibitors, Trypsin Inhibitors isolation & purification, Trypsin Inhibitors pharmacology, Vegetables analysis, Protease Inhibitors
- Abstract
A proteinase inhibitor was isolated and partially purified from the exocarp of eggplant, Solanum melongena L., by means of acetate buffer extraction, heat treatment, salting-out and column chromatography on DEAE-cellulose. This preparation showed inhibitory activities on various proteinases; trypsin [EC 3.4.4.4] and Pronase were strongly inhibited while alpha-chymotrypsin [EC 3.4.4.5] and Nagarse were weakly inhibited. The inhibitor was a protein substance, and, therefore, it was gradually inactivated by the long-time incubation with Pronase. The inhibition mode was non-competitive on trypsin and competitive on Pronase on the basis of Lineweaver-Burk plots. The investigations on the inhibition behavior in the co-existence of two kinds of proteinases suggested that the inhibitor was not of multi-headed type.
- Published
- 1975
- Full Text
- View/download PDF
42. Isolation and characterization of trypsin inhibitor from opaque-2 corn seeds.
- Author
-
Swartz MJ, Mitchell HL, Cox DJ, and Reeck GR
- Subjects
- Chromatography, Affinity, Molecular Weight, Zea mays analysis, Plants analysis, Trypsin Inhibitors isolation & purification
- Abstract
Trypsin inhibitor was isolated from seeds of opaque-2 corn by affinity chromatography on a trypsin/Sepharose column. The two major forms of inhibitor eluted from the affinity column were separated by DEAE-cellulose chromatography in the presence of urea. One form of inhibitor is a single-chain protein that has a molecular weight of approximately 12,500; the second inhibitor has two polypeptide chains and appears to have been produced from the single-chain inhibitor by exposure to trypsin in the affinity chromatography step. The relationship of the inhibitor isolated from opaque-2 corn to an inhibitor previously isolated from an unspecified strain of maize by Hochstrasser et al. (Hochstrasser, K., Muss, M., and Werle, E. (1967) Z. Physiol. Chem. 348, 1337-1340) is discussed.
- Published
- 1977
43. A comparison of the dye-binding and fluorodinitrobenzene methods for determining reactive lysine in leaf-protein concentrates.
- Author
-
Walker AF
- Subjects
- England, Food Handling, Medicago sativa analysis, Methods, Poaceae analysis, Protein Binding, Coloring Agents, Dinitrofluorobenzene, Lysine analysis, Nitrobenzenes, Plant Proteins, Plants analysis
- Abstract
1. Twenty-eight leaf-protein concentrate (LPC) samples, subjected to different thermal treatments, were produced from five curd batches. For these samples, the fluorodinitrobenzene (FDNB)-reactive lysine values gave closer agreement with dye-binding lysine (DBL) than with the dye-binding capacity (DBC). 2. No relationship was established between the dye-bound-after-propionylation (DBAP) and the histidine + arginine value. 3. Comparison of dye-bound-protein values with those for tungstic-acid-precipitated nitrogen x 6.25 for the LPC samples showed the heat-damaged samples to lie below the regression line for the other samples. 4. Reactive-lysine values by dye-binding and by FDNB methods correlated well with total lysine, but the slopes of the regression line indicated closer agreement for values for samples not damaged by heat. 5. The correlation coefficients between DBC and total basic amino acids, DBC and histidine + arginine + DBL, and DBC and histidine + arginine + FDNB-reactive lysine were similar. 6. There was no correlation between the lightness of colour of the LPC samples and the availability of lysine.
- Published
- 1979
- Full Text
- View/download PDF
44. An improved method for the purification of eggplant trypsin inhibitor.
- Author
-
Ibuki F, Yamada M, Tashiro M, and Kanamori M
- Subjects
- Amino Acids analysis, Chemical Phenomena, Chemistry, Dialysis, Molecular Weight, Trypsin Inhibitors pharmacology, Plants analysis, Trypsin Inhibitors isolation & purification
- Abstract
The trypsin inhibitor in eggplant, Solanum melongena L., was isolated and purified by the improved method with the techniques of dialysis using acetylated cellulose tube and ion-exchange chromatography on DEAE-Sephadex. The final preparation was found to be homogeneous by disc and SDS-polyacrylamide gel electrophoresis. This inhibitor had the molecular weight of about 6,200, the pI value of 4.7, and furthermore characteristic amino acid composition lacking in tryptophan, histidine, valine and methionine. The trypsin inhibition data indicated that the purified inhibitor combined with bovine trypsin [EC 3.4.21.4] in the molar ratio of 1:1. These properties of this inhibitor were in agreement with those of the dialyzable eggplant trypsin inhibitor previously purified, indicating that the dialyzable and non-dialyzable inhibitors in eggplant are identical.
- Published
- 1977
- Full Text
- View/download PDF
45. The nucleotide sequences of two glycine tRNAs from Lupinus luteus seeds.
- Author
-
Barciszewska M, Barciszewski J, Kuchino Y, and Nishimura S
- Subjects
- Base Sequence, Plants analysis, RNA, Transfer, Amino Acyl analysis
- Published
- 1986
- Full Text
- View/download PDF
46. Extensive homology between the subunits of the phytohemagglutinin mitogenic proteins derived from Phaseolus vulgaris.
- Author
-
Miller JB, Hsu R, Heinrikson R, and Yachnin S
- Subjects
- Amino Acid Sequence, Amino Acids analysis, Carboxypeptidases, Peptide Fragments analysis, Plant Lectins, Plants analysis, Trypsin, Lectins
- Abstract
The phytohemagglutinin mitogenic proteins derived from Phaseolus vulgaris comprise a class of five glycoproteins that are isomeric tetramers composed of varying proportions of two different subunits (L and R). Within the native tetramer, the L subunit is a potent leukoagglutinin and mitogen that lacks hemagglutinating properties, whereas the R subunit is a potent hemagglutinin with little or no mitogenic activity. The subunits have been isolated in homogeneous form by isoelectric focusing in 8 M urea. Previous work has shown that they have equal molecular weights and differ in amino-acid sequence from residues 1-7, but are identical in positions 8-24 [(1973) J. Exp. Med. 138, 939-951]. We now report amino-acid composition studies which reveal striking similarities between the subunits. Both lack methionine and cysteine. The twelfth residue in each subunit is a glycosylated asparagine, with the identical carbohydrate composition in each. The last three residues of the subunits, as determined by carboxypeptidase A digestion, are identical. Tryptic peptide mapping of the succinylated phytohemagglutinin subunits reveals a high degree of similarity. We conclude that the substantial difference in biological properties among the tetrameric phytohemagglutinin mitogens is a result of relatively restricted differences in the primary structure of their constituent subunits.
- Published
- 1975
- Full Text
- View/download PDF
47. The presence of covalently linked ribonucleotides in the closed circular deoxyribonucleic acid from higher plants.
- Author
-
Kolodner R, Warner RC, and Tewari KK
- Subjects
- Alkaline Phosphatase, Cytoplasm analysis, Deoxyribonucleases, Drug Stability, Genes, Molecular Weight, Muramidase, Nucleic Acid Denaturation, Species Specificity, DNA, Circular, Plants analysis, Ribonucleotides analysis
- Abstract
Single-stranded scissions are induced in the covalently closed circular chloroplast (ct-) DNAs from peas, spinach, and lettuce plants by treatment with alkali or by incubation with a mixture of ribonucleases A and T1. These scissions are due to the presence of covalently linked ribonucleotides in these closed circular DNAs. By comparing the scission rates of these ctDNAs to the scission rate of RNA, it has been estimated that pea and spinach ctDNAs contain a maximum of 18 +/- 2 ribonucleotides/molecule, while lettuce ctDNA contains a maximum of 12 +/- 2 ribonucleotides/molecule. Further studies with pea ctDNA by electron microscopic methods have shown that pea ctDNA contains 19 alkali-labile sites at specific locations. A map of the relative positions of the alkali-labile sites has been constructed. These alkali-labile sites are presumably due to the insertion of individual ribonucleotides.
- Published
- 1975
48. Influence of saponins on gut permeability and active nutrient transport in vitro.
- Author
-
Johnson IT, Gee JM, Price K, Curl C, and Fenwick GR
- Subjects
- Animals, Biological Transport drug effects, Electrochemistry, Intestinal Mucosa drug effects, Kinetics, Male, Plants analysis, Polyethylene Glycols metabolism, Rats, Rats, Inbred Strains, Glycine max, Tomatine pharmacology, Cell Membrane Permeability drug effects, Galactose metabolism, Glucose metabolism, Intestinal Mucosa metabolism, Saponins pharmacology
- Abstract
The influence of four saponins, three triterpenoid glycosides and one steroidal amine glycoside, upon intestinal transport was investigated in vitro. In the presence of Gypsophylla saponin, carrier-mediated galactose transport was inhibited, although the uptake of the passively transported L-isomer of glucose increased. The uptake of the extracellular space marker, polyethylene glycol 4000, was also higher, indicating that the saponin inhibited active transport by increasing the general permeability of the enterocytes. Gypsophylla saponin, in contact only with the mucosal surface of everted jejunal sacs, induced a rapid decline in glucose-stimulated transmural potential difference. The rate of decline increased as the saponin concentration was raised over the approximate range of 0.3 to 8 mM. Saponaria saponin and alpha-tomatine also reduced transmural potential difference, but soya saponins were much less effective. The results indicate that some saponins readily increase the permeability of the small intestinal mucosal cells, thereby inhibiting active nutrient transport, and facilitating the uptake of materials to which the gut would normally be impermeable.
- Published
- 1986
- Full Text
- View/download PDF
49. DNA, RNA and protein content of tissue during growth and embryogenesis in wild-carrot suspension cultures.
- Author
-
Verma DC and Dougall DK
- Subjects
- 2,4-Dichlorophenoxyacetic Acid pharmacology, DNA analysis, Plants analysis, Plants drug effects, Plants metabolism, RNA analysis, Seeds analysis, Seeds drug effects, Seeds growth & development, Seeds metabolism, Culture Techniques, Plant Development, Plant Proteins analysis
- Abstract
A highly selected population of cells (clumps from 63 to 125 micron in diameter), obtained by screening 14-day-old stock suspension cultures of wild carrot (Daucus carota L.), was used to initiate cultures in this study. Time-course changes in DNA, RNA and protein were followed when these cultures were grown in the presence or absence of 2.25 muM 2,4-dichlorophenoxyacetic acid (2,4-D). The data show that growth of these cultures, particularly in the early part of the growth curve, is different from that in most other studies reported on suspension cultures initiated without screening. The gross compositional analysis shows that this difference stems from the very high RNA:DNA and protein: DNA ratios of the cellular material used as the inoculum in this study. The presence of 2,4-D in the medium promoted total RNA and protein levels. Correlations were sought between the appearance of embryos in the absence of exogenous 2,4-D and gross compositional differences developing in cultures grown in the presence and absence of 2,4-D. The handling of cultures during inoculation appeared to have led to a substantial loss of DNA. This had, however, little effect on dry weight or protein content of the tissue.
- Published
- 1978
- Full Text
- View/download PDF
50. Fluoride distribution and transport along rivers in the French Alps.
- Author
-
Kudo A, Garrec JP, and Plebin R
- Subjects
- Aluminum, France, Industry, Plants analysis, Water Supply analysis, Fluorides analysis, Water Pollutants analysis, Water Pollutants, Chemical analysis
- Abstract
Fluoride concentrations in water, sediments, and plants were determined at 26 locations along five rivers in the French Alps where aluminum factories have been discharging fluoride into the surrounding environment since the end of the last century. Despite a wide range of biological and constructional damages caused by fluoride contamination in the past, there was no alarming level of fluoride found in the water, sediments, or plants. Fluoride concentration in water ranged from 0.11 ppm (considered to be natural background level) to 0.62 ppm (moderate contamination). The highest fluoride concentration was 360 ppm in sediments and 207 ppm in plants. The increase of fluoride concentration along the rivers was gradual from upstream to downstream. This gradual increase suggested that the fluoride pathway was from factory to stack, to air, to the entire valley, and to the river. The amount of fluoride transported from the Maurienne valley by the Arc river was estimated to be 680 tons per year. Of this 97.8% tons (665 tons) was transported by the flowing water and the rest (2.2% or 15 tons) by sediments moving downstream.
- Published
- 1987
- Full Text
- View/download PDF
Catalog
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.