21 results on '"Addeo, F."'
Search Results
2. Fractionation of whole casein on hydroxyapatite. Application to a study of buffalo κ-casein.
- Author
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Addeo, F., Chobert, J.-M., and Ribadeau-Dumas, B.
- Published
- 1977
- Full Text
- View/download PDF
3. Primary structure of water buffalo alpha-lactalbumin variants A and B.
- Author
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Chianese L, Caira S, Lilla S, Pizzolongo F, Ferranti P, Pugliano G, and Addeo F
- Subjects
- Alleles, Animals, Chromatography, High Pressure Liquid, Gene Frequency, Glycosylation, Immunoblotting, Isoelectric Focusing, Lactalbumin genetics, Milk Proteins chemistry, Molecular Sequence Data, Spectrometry, Mass, Electrospray Ionization, Whey Proteins, Amino Acid Sequence, Buffaloes, Genetic Variation, Lactalbumin chemistry
- Abstract
A novel electrophoretic alpha-lactalbumin (alpha-la) variant was detected in the Italian water buffalo breed. The isoelectric point of the variant, labelled A, was lower than the most frequent variant B. It presented an allelic frequency of 0.5% compared with the 97.1% of the BB allele. From Liquid Chromatography-Electrospray Ionization/Mass spectrometry, the molecular mass of the two alpha-la A and B variants were measured as 14,235.1+/-0.8 and 14,236.1+/-0.9 Da, respectively. The two proteins were sequenced and differentiated from one another by a single amino acid substitution, Asn45(B)-->Asp45(A). As this amino acid substitution altered the N-glycosylation sequence consensus Asn45-X-Ser46 it may be deduced that the protein glycosylation level of the alpha-la A would decrease.
- Published
- 2004
- Full Text
- View/download PDF
4. Casein proteolysis in human milk: tracing the pattern of casein breakdown and the formation of potential bioactive peptides.
- Author
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Ferranti P, Traisci MV, Picariello G, Nasi A, Boschi V, Siervo M, Falconi C, Chianese L, and Addeo F
- Subjects
- Amino Acid Sequence, Caseins analysis, Caseins chemistry, Chromatography, High Pressure Liquid, Dimerization, Endopeptidases metabolism, Exopeptidases metabolism, Female, Fibrinolysin metabolism, Humans, Infant, Newborn, Infant, Premature, Lysine metabolism, Mass Spectrometry, Milk, Human enzymology, Molecular Sequence Data, Peptide Mapping, Sequence Analysis, Protein, Solubility, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Trichloroacetic Acid, Caseins metabolism, Milk, Human chemistry, Peptides analysis
- Abstract
The protein and peptide fraction of human milk samples collected from mothers of pre- and full-term infants in the first week after parturition was analysed by use of liquid chromatography-mass spectrometry and tandem mass spectrometry. By characterising the peptide sequence, we defined the pathway of casein hydrolysis which leads to the formation of small peptides through intermediate oligopeptides. It was found that the action of a plasmin-like enzyme acting on specific lysine residues is the primary step in casein degradation. This is followed by endopeptidases and/or exopeptidases mediated cleavage of the oligopeptides which, in turn, produces a multiplicity of short peptides differing by one or more amino acid residues. In this process, a series of potentially bioactive peptides (opioid, phosphopeptides) and their precursors are produced.
- Published
- 2004
- Full Text
- View/download PDF
5. Synthetic peptides as substrate for assaying the proteolytic activity of Lactobacillus helveticus.
- Author
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Caira S, Ferranti P, Gatti M, Fornasari ME, Barone F, Lilla S, Mucchetti G, Picariello G, Chianese L, Neviani E, and Addeo F
- Subjects
- Amino Acids metabolism, Aminopeptidases metabolism, Cell Wall enzymology, Cell Wall metabolism, Chromatography, Liquid, Cytoplasm enzymology, Food Microbiology, Hydrolysis, Mass Spectrometry, Peptides chemical synthesis, Substrate Specificity, Cheese microbiology, Lactobacillus enzymology, Peptide Hydrolases metabolism, Peptides metabolism
- Abstract
Four Lactobacillus helveticus strains were studied for proteolytic capacity and general aminopeptidase (AP) and X-Pro dipeptidyl aminopeptidase (DAP) activity. The rate of hydrolysis and the activity against synthetic substrates with N-terminal residues of Arg, Lys, Leu, Glu or Pro, varied markedly among the strains. The X-Pro DAP activity was consistently high. The crude cell-wall and cytoplasm extracts from strain Lb. helveticus ISLC59 were analysed thoroughly for their proteolysis ability by using four synthetic peptide substrates, including alpha(s)1-CN(f1-23). Peptides formed during in vitro hydrolysis of the synthetic substrates by cell wall and cytoplasm preparations were identified by LC-ESI/MS. In doing so, it was possible to infer a prevalent endopeptidase activity splitting Lys7-His8 and Gln13-Glu14 bonds in the cytoplasm, and to deduce a secondary activity, which hydrolysed Glu14-Val15, Leu16-Asn17, Glu18-Asn19 and Lys3-His4 bonds lacking in the cell-wall. The presence of exopeptidases, as mainly AP, DAP, and carboxypeptidase (CPase) was deduced from the formation of several N- and C-terminally truncated peptides sets. The AP activity was higher in the cell-wall layer, where CPase activity was absent. The in vitro assays with cell extracts of the Lb. helveticus ISLC59 strain revealed extensive exopeptidase and endopeptidase activities. In several cases, the hydrolytic system of Lb. helveticus that splits in vitro alpha(s)1-CN(f1-23) peptide bonds was similar to that of Lactococcus lactis. The effects were also compared with those occurring in vivo in hard cheese such as Grana Padano.
- Published
- 2003
- Full Text
- View/download PDF
6. Mass spectrometry-based procedure for the identification of ovine casein heterogeneity.
- Author
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Ferranti BP, Pizzano R, Garro G, Caira S, Chianese L, and Addeo F
- Subjects
- Animals, Caseins chemistry, Chromatography, High Pressure Liquid, Electrophoresis, Capillary, Milk Proteins analysis, Milk Proteins chemistry, Spectrometry, Mass, Electrospray Ionization, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Caseins analysis, Sheep metabolism
- Abstract
The efficiency of reversed-phase HPLC, capillary electrophoresis (CE), PAGE and isoelectric focusing with immunoblotting in separating ovine caseins has been evaluated. The assessment was carried out by employing electrospray ionization-mass spectrometry (ESI-MS) and matrix-assisted laser desorption ionization-time of flight as reference tools for identifying protein components. Ovine casein was fractionated by HTPC into four major peaks. With ESI-MS, each peak contained components belonging to only one of the four casein families. On-line liquid chromatography-ESI-MS allowed us to determine each fraction's composition by detecting thirteen alphas1-, eleven alphas2-, seven beta-, and three kappa-casein (CN) components. The alphas1-CN and alphas2-CN consisted of eight and two protein chains respectively of lengths differing through the deletion of one or more peptide sequences; they were also discretely phosphorylated as kappa-CN and beta-CN. By CE at pH 2.5, each casein fraction was as heterogeneous as that resulting from ESI-MS for the single HPLC-derived fractions. The separation of alphas1-CN and alphas2-CN proved to be excellent, with the exception of a co-migration of kappa0-CN with a minor alphas1-CN component and of a glycosylated kappa-CN for with low-phosphorylated = alphas1-CN and beta-CN components. Dephosphorylation of whole casein was used to reduce the heterogeneity of the native fractions and by applying currently used analytical techniques it was possible to visualize the protein moiety difference along the CE profile. CE, HPLC, and immunoblotting were all equally capable of effecting an accurate separation of the four dephosphorylated casein families. The spectra obtained by ESI-MS directly on dephosphorylated whole ovine casein samples contained the signals of the four casein families and the relative alphas1-CN variants, the non-allelic alphas1-CN and alphas2-CN forms, dimeric kappa-CN and other newly formed peptides. We suggest using this procedure for rapid characterization of whole casein.
- Published
- 2001
- Full Text
- View/download PDF
7. Odour-impact compounds of Gorgonzola cheese.
- Author
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Moio L, Piombino P, and Addeo F
- Subjects
- Animals, Anisoles analysis, Caproates analysis, Cattle, Chromatography, Gas, Gas Chromatography-Mass Spectrometry, Heptanol analysis, Ketones analysis, Octanols analysis, Volatilization, Cheese analysis, Odorants
- Abstract
Volatile concentrates were obtained by vacuum distillation from both natural and creamy Gorgonzola cheese and isolated by continuous liquid-liquid extraction. Both were analysed by high resolution gas chromatography (HRGC), HRGC-mass spectrometry and HRGC-olfactometry. A total of 63 components were identified in the neutral extract of the natural type (21 esters, 13 ketones, 14 alcohols, 5 aldehydes, 1 sulphur compound, 7 aromatic compounds and 2 terpenes) and 52 in the creamy type (17 esters, 12 ketones, 10 alcohols, 5 aldehydes, 1 sulphur compound, 5 aromatic compounds and 2 terpenes). Ketones, whose major components were 2-nonanone and 2-heptanone, were the predominant constituents of the neutral fraction. By olfactometric analysis of the neutral extracts, 23 odour-impact compounds were found in the natural and 21 in the creamy Gorgonzola cheese. 1-Octen-3-ol, ethyl hexanoate, 2-nonanone, 2-heptanone, 2-heptanol, ethyl butanoate, 2-nonanol and 4-methylanisole were the key odorants of the natural cheese, whereas 2-heptanone, 2-heptanol, ethyl butanoate, 3-methyl thiopropanal and an unidentified constituent with a fruity odour were characteristic of the creamy Gorgonzola cheese. On the basis of high odour unity values, 2-nonanone, 1-octen-3-ol, 2-heptanol, ethyl hexanoate, methylanisole and 2-heptanone were the most important odorants of natural and creamy Gorgonzola cheese aroma.
- Published
- 2000
- Full Text
- View/download PDF
8. Isolation of specific oligoclonal antibodies against bovine alpha s1-casein by FPLC tandem immunoaffinity of the polyclonal antibodies.
- Author
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Moio L, Marchisano C, and Addeo F
- Subjects
- Animals, Antibodies immunology, Antibody Specificity, Cattle, Chromatography, Affinity, Female, Immunoblotting, Immunologic Techniques, Isoelectric Focusing, Antibodies isolation & purification, Caseins analysis, Caseins immunology, Chromatography, High Pressure Liquid methods
- Published
- 1998
- Full Text
- View/download PDF
9. Identification of C-terminally truncated forms of beta-lactoglobulin in whey from Romagnola cows' milk by two dimensional electrophoresis coupled to mass spectrometry.
- Author
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Zappacosta F, Di Luccia A, Ledda L, and Addeo F
- Subjects
- Amino Acid Sequence, Animals, Cattle, Electrophoresis, Gel, Two-Dimensional, Female, Isoelectric Focusing, Lactoglobulins genetics, Lactoglobulins isolation & purification, Mass Spectrometry, Molecular Sequence Data, Peptide Fragments chemistry, Peptide Fragments isolation & purification, Sensitivity and Specificity, Trypsin, Whey Proteins, Genetic Variation, Lactoglobulins chemistry, Milk chemistry, Milk Proteins chemistry, Sequence Deletion
- Abstract
Four minor protein components were detected in whey from Romagnola cows' milk by polyacrylamide gel isoelectric focusing and two dimensional gel electrophoresis. Individual protein spots were transferred by electroblotting on to a polyvinylidene difluoride membrane and isolated by cutting out the relevant area. After in situ trypsinolysis, a portion of the digest was analysed directly by matrix-assisted laser desorption ionization-time of flight mass spectrometry. The mass profile allowed us to establish a correlation between beta-lactoglobulins A and B and the four minor whey protein components. They were identified as C-terminally truncated beta-lactoglobulin A and B variants with missing N-terminal peptides, beyond residues in the range 100-123 and 136-147 respectively. Two of the minor components were related to beta-lactoglobulin A and two to beta-lactoglobulin B.
- Published
- 1998
- Full Text
- View/download PDF
10. Phosphopeptides from Grana Padano cheese: nature, origin and changes during ripening.
- Author
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Ferranti P, Barone F, Chianese L, Addeo F, Scaloni A, Pellegrino L, and Resmini P
- Subjects
- Amino Acid Sequence, Barium, Carboxypeptidases metabolism, Caseins chemistry, Caseins isolation & purification, Caseins metabolism, Chemical Precipitation, Chromatography, High Pressure Liquid, Fibrinolysin metabolism, Hydrogen-Ion Concentration, Hydrolysis, Lysine analysis, Peptide Fragments analysis, Peptide Fragments chemistry, Peptide Fragments metabolism, Phosphoserine analysis, Phosphoserine metabolism, Solubility, Spectrometry, Mass, Fast Atom Bombardment, Time Factors, Trypsin metabolism, Caseins analysis, Cheese analysis, Phosphopeptides analysis
- Abstract
Casein phosphopeptides (CPP) which develop in Grana Padano cheese at different ages were isolated by precipitation with Ba2+ and analysed by HPLC. Profiles were complex throughout the period between 4 and 38 months. CPP in a cheese sample 14 months old were identified by a combination of fast atom bombardment-mass spectrometry and Edman degradation. They were found to consist of a mixture of components derived from three parent peptides, beta-CNf(7-28)4P, alpha s1-CNf(61-79)4P and alpha s2-CNf(7-21)4P. In total, 45 phosphopeptides were identified: 24 from beta-CN, 16 from alpha s1-CN and 5 from alpha s2-CN. The presence of aminopeptidase activity during cheese ripening was deduced from the presence of a number of CPP of different lengths with the loss of one or more residues from the N-terminus. The longest had C-terminal lysine and seemed to be progressively hydrolysed by carboxypeptidases A and B to shorter peptides. CPP in cheese appeared to be shortened plasmin-mediated products. Moreover, those most resistant to further hydrolysis contained at least three closely located phosphoserine residues. The anticariogenic activity of CPP is also discussed.
- Published
- 1997
- Full Text
- View/download PDF
11. Occurrence of five alpha s1-casein variants in ovine milk.
- Author
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Chianese L, Garro G, Mauriello R, Laezza P, Ferranti P, and Addeo F
- Subjects
- Animals, Chromatography, High Pressure Liquid, Electrophoresis, Gel, Two-Dimensional, Electrophoresis, Polyacrylamide Gel, Female, Hydrogen-Ion Concentration, Immunoblotting, Isoelectric Focusing, Italy, Mass Spectrometry, Caseins analysis, Milk chemistry, Sheep
- Abstract
Five ovine alpha s1-casein variants (A-E) were identified in an Italian population sample using gel electrophoresis at alkaline pH, gel isoelectric focusing, two dimensional gel electrophoresis, and immunoblotting with polyclonal antibodies against alpha s1-casein. Each casein sample produced two peaks by fast reversed-phase HPLC. Gel isoelectric focusing and electrospray mass spectrometry were used to demonstrate that the first HPLC peak contained the 191 residue alpha s1-casein molecular species and the second the 199 residue species, in proportions of approximately 20:80. Only in the case of the sample containing alpha s1-casein CE was the method for the separation of the single short and long forms of each variant unsuccessful. Both two dimensional electrophoresis followed by staining with polyclonal antibodies against alpha s1-casein and electrospray mass spectrometry showed a heterogeneity consistent with that expected from a protein chain with three levels of phosphorylation and two different lengths. However, especially for alpha s1-caseins D and E, a further uncharacterized heterogeneity was detected.
- Published
- 1996
- Full Text
- View/download PDF
12. Primary structure of ovine alpha s1-caseins: localization of phosphorylation sites and characterization of genetic variants A, C and D.
- Author
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Ferranti P, Malorni A, Nitti G, Laezza P, Pizzano R, Chianese L, and Addeo F
- Subjects
- Amino Acid Sequence, Animals, Binding Sites, Caseins genetics, Caseins metabolism, Cattle, Chromatography, High Pressure Liquid, Molecular Sequence Data, Peptide Fragments chemistry, Peptide Fragments isolation & purification, Peptide Mapping, Phosphorylation, Phosphoserine metabolism, Spectrometry, Mass, Fast Atom Bombardment, Trypsin metabolism, Caseins chemistry, Genetic Variation, Phosphates metabolism
- Abstract
The primary structures of ovine alpha s1-casein variants A, C and D (formerly called Welsh variant) were determined. Separation of variants from whole casein was achieved using a fast and reliable reversed-phase HPLC method. Extended structural characterization of the purified proteins using electrospray mass spectrometry, automated Edman degradation and peptide mapping by means of HPLC-fast atom bombardment-mass spectrometry demonstrated that the mature protein was a mixture of two molecular species that differed in the deletion of residues 141-148 and were therefore 199 and 191 residues long respectively. The 199 residue peptide chain, which accounted for approximately 80% of the entire translated alpha s1-casein, was as long as its caprine and bovine counterparts, and had a 98 and 89% degree of identity with those two proteins respectively. Nine serine residues (positions 12, 44, 46, 64 to 68 and 75) were fully phosphorylated in alpha s1-casein A, whereas Ser115 and Ser41 were phosphorylated by approximately 50 and approximately 20% respectively. The differences between the three genetic variants A, C and D were simple silent substitutions, which however involved the degree to which the protein was phosphorylated. Variant C differed from variant A in the substitution Ser13-->Pro13 which determined the loss of the phosphate group on site 12 of the protein chain, SerP12-->Ser12. A further substitution, SerP68-->Asn68 caused the disappearance of both phosphate groups in the phosphorylated residues Ser64 and Ser66 in variant D; in this last casein variant there was no evidence of phosphorylation at Ser41.
- Published
- 1995
- Full Text
- View/download PDF
13. Gel electrophoresis and immunoblotting for the detection of casein proteolysis in cheese.
- Author
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Addeo F, Garro G, Intorcia N, Pellegrino L, Resmini P, and Chianese L
- Subjects
- Amino Acid Sequence, Caseins analysis, Chymosin metabolism, Fibrinolysin metabolism, Hydrogen-Ion Concentration, Isoelectric Focusing, Molecular Sequence Data, Peptide Fragments chemistry, Caseins metabolism, Cheese analysis, Electrophoresis, Polyacrylamide Gel, Endopeptidases metabolism, Immunoblotting, Peptide Fragments analysis
- Abstract
The whole N fraction of six samples of hard and semi-hard pressed cheeses was analysed using PAGE, polyacrylamide gel isoelectric focusing and immunoblotting with polyclonal antibodies against beta- and alpha s1-casein. The origin of some electrophoretic bands corresponding to peptides produced from the enzymic degradation of the casein fractions was established. A number of these peptides were also present in the in vitro hydrolysates of casein with plasmin and chymosin. Thus, it was also possible to determine which casein was the source of each peptide and which enzymes were active in cheese. Compared with the traditional Coomassie staining procedures, immunoblotting is more sensitive and specific, making the interpretation of each electrophoretic profile easy. Thus, it was also possible to obtain a clear picture of the state of each casein fraction in a cheese variety. Two main peptides were isolated from the pH 4.6-insoluble N fraction of Parmigiano-Reggiano using DEAE-cellulose chromatography and identified, from the amino acid sequence of the N- and C-terminal ends, as gamma 3-casein (beta-casein(f108-209)) and alpha s1-PL1 (alpha s1-casein(f80-199). In both cases, a Lys-X bond was hydrolysed, indicating the action of a trypsin-like enzyme in beta- and alpha s1-casein hydrolysis during the ripening of this variety of hard pressed cheese.
- Published
- 1995
- Full Text
- View/download PDF
14. Characterization of the oligopeptides of Parmigiano-Reggiano cheese soluble in 120 g trichloroacetic acid/l.
- Author
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Addeo F, Chianese L, Sacchi R, Musso SS, Ferranti P, and Malorni A
- Subjects
- Amino Acid Sequence, Chromatography, High Pressure Liquid, Molecular Sequence Data, Molecular Weight, Oligopeptides chemistry, Phosphopeptides analysis, Phosphopeptides chemistry, Spectrometry, Mass, Fast Atom Bombardment, Cheese analysis, Oligopeptides analysis
- Abstract
The non-protein nitrogen (NPN) of samples of Parmigiano-Reggiano cheese ripened for 6 and 15 months was fractionated by ion-exchange chromatography on a Cu(2+)-Chelex column to separate oligopeptides from free amino acids. Peptide components were isolated by reversed-phase HPLC and identified by fast atom bombardment-mass spectrometry (FAB-MS). Only the NPN fraction of 6 month old cheese samples contained enough peptides to be further characterized. On the basis of FAB-MNS spectral results, 39 oligopeptides were identified, the main components being phosphopeptides. Two sets of both intact and partly dephosphorylated peptides, accounting for a total of 19 phosphopeptides, were formed by the hydrolysis of beta-casein and belonged to regions 1-20 and 6-28 of beta-casein. The formation and potential role of these peptides in cheese is discussed.
- Published
- 1994
- Full Text
- View/download PDF
15. Discovery of an ovine alpha S2-casein variant.
- Author
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Chianese L, Garro G, Addeo F, Lopez-Galvez G, and Ramos M
- Subjects
- Animals, Caseins chemistry, Electrochemistry, Electrophoresis, Gel, Two-Dimensional, Electrophoresis, Polyacrylamide Gel, Female, Hydrogen-Ion Concentration, Immunoblotting, Isoelectric Point, Caseins isolation & purification, Genetic Variation, Milk chemistry, Sheep
- Abstract
A novel ovine alpha S2-casein variant has been detected using discontinuous polyacrylamide gel electrophoresis at alkaline pH, two dimensional electrophoresis and immunoblotting. It is characterized by a greater negative net charge and a lower isoelectric point compared with the most common ovine alpha S2-casein variant. The phenotypic frequency in the Manchega breed is 5.5%.
- Published
- 1993
- Full Text
- View/download PDF
16. New alpha s2-casein variant from caprine milk.
- Author
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Chianese L, Mauriello R, Intorcia N, Moio L, and Addeo F
- Subjects
- Animals, Chromatography, Electrophoresis, Polyacrylamide Gel, Female, Hydrogen-Ion Concentration, Immunoblotting, Isoelectric Focusing, Caseins analysis, Genetic Variation, Goats metabolism, Milk chemistry
- Abstract
A new alpha s2-casein variant was isolated from goat milk by means of covalent chromatography. With gel electrophoresis at alkaline pH, the alpha s2-casein variant showed a double band with the highest anodic mobility amongst the casein components. The mobility of the isolated alpha s2-casein variant was similar to that occurring in three individual samples of whole casein. Two dimensional electrophoresis revealed a more pronounced heterogeneity of this protein. Developing the two dimensional plate with polyclonal antibodies obtained against the four main bovine casein fractions, we demonstrated that the variant in question belongs to the alpha s2-casein family. Since the alpha s2-casein fractions, immunospecifically developed, spread along two different zones on the gel, it was concluded that a heterozygous alpha s2-casein form was present in the sample.
- Published
- 1992
- Full Text
- View/download PDF
17. Determination of ovine casein heterogeneity using gel electrophoresis and immunochemical techniques.
- Author
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Chianese L, Mauriello R, Moio L, Intorcia N, and Addeo F
- Subjects
- Animals, Densitometry, Electrophoresis, Disc, Electrophoresis, Gel, Two-Dimensional, Electrophoresis, Polyacrylamide Gel, Hydrogen-Ion Concentration, Immunoblotting, Isoelectric Focusing, Sheep, Caseins chemistry, Milk analysis
- Abstract
Discontinuous PAGE at alkaline and acid pH, polyacrylamide gel isoelectric focusing, two dimensional electrophoresis and immunoblotting have been used to study the heterogeneity of sheep caseins. Three main phenotypes were selected either because of mobility at alkaline and acid pH of the individual alpha s components or because of their relative intensity. On electrophoresis at alkaline pH, one phenotype showed two distinct bands of lower electrophoretic mobility than beta 1- and beta 2-caseins. A detailed study of these components using immunospecific detection with beta-casein antiserum showed that these minor components of ovine casein may have a polypeptide chain similar to that of beta 1- and beta 2-caseins. Complete electrophoretic patterns of the casein components in some individual milks are also presented.
- Published
- 1992
- Full Text
- View/download PDF
18. Specific action of milk-clotting enzymes on water buffalo caseins. I. Effect of chymosin on beta-casein.
- Author
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Addeo F, Pelissier JP, and Chianese L
- Subjects
- Animals, Buffaloes, Models, Chemical, Caseins metabolism, Chymosin pharmacology
- Published
- 1980
- Full Text
- View/download PDF
19. Buffalo alpha S0-casein: isolation and characterization.
- Author
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Petrilli P, Chianese L, and Addeo F
- Subjects
- Amino Acids analysis, Animals, Buffaloes, Cattle, Female, Pregnancy, Species Specificity, Caseins isolation & purification
- Abstract
A method for the preparation of alpha S0-casein, and for the preparation of alpha S1-casein fractions 1 and 2 from buffalo casein are described. The amino acid composition and phosphorus content of alpha S0-casein are given and compared with those of other alphaS-caseins.
- Published
- 1979
- Full Text
- View/download PDF
20. Fractionation of whole casein on hydroxyapatite. Application to a study of buffalo kappa-casein.
- Author
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Addeo F, Chobert JM, and Ribadeau-Dumas B
- Subjects
- Animals, Chromatography, Chromatography, DEAE-Cellulose, Female, Hydroxyapatites, Milk analysis, Buffaloes metabolism, Caseins isolation & purification
- Abstract
When whole caseins from cow and Italian buffalo (Bubalus arnee) were fractionated by chromatography on a column of hydroxyapatite they behaved in a similar manner. kappa-Casein was eluted with 5 mM phosphate buffer, pH 6-8, containing 0-2 M-KCl, 4-5 M-urea and 2 mM-2-mercaptoethanol, but beta- and alphas-caseins were retained and could be eluted successively by a linear gradient from 5 mM to 250 mM-phosphate buffer. Buffalo kappa-casein preparations, obtained from bulk milk or from milks of individual animals by chromatography on hydroxyapatite, produced identical electrophoretic patterns at pH 8-6. By further fractionation of these kappa-caseins on DEAE-cellulose, in each case, at least 7 components were purified; they had different electrophoretic mobilities but were all sensitive towards chymosin. The major fraction migrated like component 1 of bovine kappa-casein B.
- Published
- 1977
- Full Text
- View/download PDF
21. Preparation and fractionation of goat kappa-casein: analysis of the glycan and peptide components.
- Author
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Addeo F, Soulier S, Pelissier JP, Chobert JM, Mercier JC, and Ribadeau-Dumas B
- Subjects
- Animals, Caseins isolation & purification, Chromatography, DEAE-Cellulose, Electrophoresis, Polyacrylamide Gel, Female, Milk analysis, Caseins analysis, Goats metabolism, Peptides analysis, Polysaccharides analysis
- Abstract
Whole goat kappa-casein was prepared by chromatography of whole casein on hydroxyapatite. Chromatography of whole kappa-casein on DEAE-cellulose separated 5 fractions. All of them were sensitive to chymosin. Their amino acid and carbohydrate composition, phosphate content and molecular weight were determined. Galactose, N-acetylgalactosamine, N-acetyl and N-glycolyl neuraminic acids were identified in whole kappa-casein. It appears that goat kappa-casein, like cow, buffalo and ewe kappa-caseins, is composed of several fractions having identical peptide chains and differing in their carbohydrate contents. The main fraction, devoid of carbohydrate, was treated with chymosin. The para-kappa-casein and caseinomacropeptide were isolated. Their amino acid composition and phosphate content were determined.
- Published
- 1978
- Full Text
- View/download PDF
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