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Start Over Topic amino acids Topic animals Journal hoppe-seyler's zeitschrift fur physiologische chemie
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2. The amino acid sequences of the alpha and beta polypeptide chains of adult hemoglobin of the capuchin monkey (Cebus apella)

Author

G, Matsuda, T, Maita, B, Watanabe, W, Araya, K, Morokuma, Y, Ota, M, Goodman, J, Barnabas, and W, Prychodko

Subjects
Dansyl Compounds, Chromatography, Chromatography, Paper, Macromolecular Substances, Thermolysin, Carboxypeptidases, Haplorhini, Hydrogen-Ion Concentration, Chromatography, Ion Exchange, Pepsin A, Peptide Fragments, Hemoglobins, Chromatography, Gel, Animals, Chymotrypsin, Electrophoresis, Paper, Trypsin, Amino Acid Sequence, Subtilisins, Amino Acids, Peptides
Published
1973

3. Preparation and application of Nalpha-B1,Nepsilon-B29-bis (ter.-butyloxycarbonyl)insulin

Author

H J, Friesen, V K, Naithani, and H G, Gattner

Subjects
Dansyl Compounds, Azides, Animals, Insulin, Trifluoroacetic Acid, Cattle, Electrophoresis, Paper, Electrophoresis, Cellulose Acetate, Amino Acids, Chromatography, Ion Exchange
Abstract

Two methods are described for the preparation of NalphaB1,Nepsilon29-Boc2-insulin from Nalpha A1-trifluoroacetyl-insulin and Nalpha A1-citraconyl-insulin in 80 - 90% and 65% yields, respectively. Removal of the Boc protections afforded the fully active insulin. Application of this derivative was demonstrated by the preparations of des-GlyA1-insulin and [A1-guanidinoacetyl]insulin. The former compount exhibited 2% activity in the in vitro free fat cell assay and the latter 88 +/- 5% while NalphaB1-NepsilonB29-Boc2-insulin showed 45 +/- 3% activity only.

Published
1978

4. Studies on the primary structures of alpha and beta polypeptide chains of adult hemoglobin of the spider monkey (Ateles geoffroyi)

Author

G, Matsuda, T, Maita, Y, Suzuyama, M, Setoguchi, Y, Ota, A, Araya, M, Goodman, J, Barnabas, and W, Prychodko

Subjects
Dansyl Compounds, Chromatography, Chromatography, Paper, Haplorhini, Chromatography, Ion Exchange, Pepsin A, Peptide Fragments, Hemoglobins, Species Specificity, Chromatography, Gel, Animals, Chymotrypsin, Humans, Trypsin, Amino Acid Sequence, Cyanogen Bromide, Subtilisins, Amino Acids, Peptides
Published
1973

5. Snake venom toxins. The purification of toxins VII1 and VII2, two cytotoxin homologues from banded Egyptian cobra (Naja haje annulifera) venom, and the complete amino acid sequence of toxin VII1

Author

K H, Weise, F H, Carlsson, F J, Joubert, and D J, Strydom

Subjects
Dansyl Compounds, Chromatography, Gas, Venoms, Snakes, Chromatography, Ion Exchange, Peptide Fragments, Mice, Species Specificity, Papain, Chromatography, Gel, Animals, Biological Assay, Electrophoresis, Paper, Spectrophotometry, Ultraviolet, Trypsin, Amino Acid Sequence, Chromatography, Thin Layer, Cyanogen Bromide, Amino Acids, Toxins, Biological
Published
1973

6. Snake venoms. The amino-acid sequence of polypeptide DE-1 from Ophiophagus hannah (King cobra) venom

Author

Francois J. Joubert

Subjects
Chemistry, King Cobra Venom, Chromatography, Paper, Size-exclusion chromatography, Protein primary structure, Sequence (biology), Chromatography, Ion Exchange, Biochemistry, Sephadex, Chromatography, Gel, Neurotoxin, Animals, Amino Acid Sequence, Amino acid residue, Amino Acids, Peptides, Peptide sequence, Snake Venoms
Abstract

A major polypeptide (DE-1) was purified from King cobra venom by ion-exchange chromatography on CM-cellulose and also DEAE-cellulose and by gel filtration on Sephadex G-50. DE-1 comprises 60 amino acid residues and is cross-linked by four intrachain disulphide bridges. The complete primary structure of the polypeptide has been elucidated. The properties of DE-1 were compared with those of the short neurotoxin and the cytotoxin groups and of the angusticeps types. The sequence and some of the invariant residues of DE-1 resemble the short neurotoxin group and to some degree also the cytotoxin group, but it is a nontoxic (LD50 greater than 250 microgram/g of mouse) polypeptide.

Published
1977

7. Studies on polypeptides. I. The synthesis of C-peptide of porcine proinsulin

Author

Vinod K. Naithani

Subjects
Swine, Biochemistry, Chromatography, DEAE-Cellulose, chemistry.chemical_compound, Benzyl Compounds, Animals, Electrophoresis, Paper, Amino Acid Sequence, Solubility, Cellulose, Amino Acids, Leucyl aminopeptidase, Nitrobenzenes, Proinsulin, chemistry.chemical_classification, C-peptide, Dimethylformamide, Esters, Peptide Chain Termination, Translational, Chromatography, Ion Exchange, Amino acid, Electrophoresis, Butyrates, chemistry, Chromatography, Thin Layer, Crystallization, Peptides
Published
1972

8. [The sequence of beta-lactoglobulin (author's transl)]

Author

G, Braunitzer, R, Chen, B, Schrank, and A, Stangl

Subjects
Autoanalysis, Chromatography, Paper, Lactoglobulins, Chromatography, Ion Exchange, Pepsin A, Peptide Fragments, Evaluation Studies as Topic, Methods, Animals, Cattle, Female, Spectrophotometry, Ultraviolet, Trypsin, Amino Acid Sequence, Cyanogen Bromide, Amino Acids, Oxidation-Reduction
Published
1973

10. [Preparation and properties of mixed disulfides of insulin with glutathione and thioglycollic acid (author's transl)]

Author

W D, Busse and H G, Gattner

Subjects
Electrophoresis, Binding Sites, Passive Cutaneous Anaphylaxis, Chromatography, Ion Exchange, Glutathione, Peptide Fragments, Evaluation Studies as Topic, Thioglycolates, Chromatography, Gel, Methods, Animals, Chymotrypsin, Insulin, Cattle, Electrophoresis, Paper, Spectrophotometry, Ultraviolet, Disulfides, Amino Acids, Cellulose, Oxidation-Reduction, Protein Binding
Published
1973

14. Selective cleavage of one disulfide bond in insulin: preparation and properties of insulin A7-B7-di-S-sulfonate

Author

Hans-Gregor Gattner and Wolf-Dieter Busse

Subjects
Blood Glucose, Protein Conformation, medicine.medical_treatment, Guinea Pigs, Plasma protein binding, Biochemistry, chemistry.chemical_compound, Mice, Protein structure, medicine, Animals, Chymotrypsin, Insulin, Urea, Electrophoresis, Paper, Disulfides, Binding site, Amino Acids, chemistry.chemical_classification, Binding Sites, biology, Chemistry, Passive Cutaneous Anaphylaxis, Fasting, Hydrogen-Ion Concentration, Chromatography, Ion Exchange, Peptide Fragments, Amino acid, Rats, Sulfonate, biology.protein, Chromatography, Gel, Biological Assay, Cattle, Sulfonic Acids, Protein Binding
Published
1973

15. Preparation and characteristics of porcine growth hormone

Author

Karl-Heinz Voigt and Mark Schleyer

Subjects
chemistry.chemical_classification, Molar concentration, Ion exchange, Tibia, Chemistry, Swine, Ion chromatography, Phenylalanine, Biological activity, Growth hormone, Biochemistry, Bone and Bones, Amino acid, Rats, Growth Hormone, Pituitary Gland, Methods, Animals, Biological Assay, Amino Acids, Hormone
Abstract

A recently published method for preparation of porcine growth hormone resulted in a highly purified protein with good biological activity. However, after storing for some months the originally homogeneous hormone separated again into several fractions when rechromatographed on ion exchange columns. The biological activity, found in one of these fractions, was clearly diminished compared with the activity of a freshly prepared hormone. In the present paper a modified procedure is described for the isolation of a more stable porcine growth hormone. The influence of ions, involved in buffers of the same molarity and the same pH, upon ion exchange chromatography of porcine growth hormone is discussed. The purified hormone shows high biological activity in the tibia test and is free of activities of other pituitary hormones. The molecular weight is about 20 000; only phenylalanine is found as N-terminal as well as C-terminal amino acid; the amino acid composition resembles neither that of porcine growth hormone described in literature nor that of human growth hormone.

Published
1979