Profiling of genetic variants of bovine κ-casein macropeptide by electrophoretic and chromatographic techniques

Bovine κ-caseins of single variant phenotype (AA and BB) and mixed phenotype (AA, BB and AB) were purified from milk and the corresponding κ-casein macropeptides prepared by chymosin hydrolysis. The macropeptides were characterized by PAGE, Mono Q- and reverse-phase HPLC. Chromatographic profiles sh...

Celý popis

Uloženo v:
Podrobná bibliografie
Vydáno v:International dairy journal Ročník 6; číslo 11; s. 1055 - 1068
Hlavní autoři: Coolbear, Kate P., Elgar, David F., Ayers, John S.
Médium: Journal Article
Jazyk:angličtina
Vydáno: Oxford Elsevier Ltd 01.11.1996
Elsevier Science
Témata:
amino acids
Analytical, structural and metabolic biochemistry
Biological and medical sciences
dairy cows
Fundamental and applied biological sciences. Psychology
galactosamine
genetic polymorphism
high performance liquid chromatography
kappa-casein
Miscellaneous
peptides
phosphates
polyacrylamide gel electrophoresis
protein composition
Proteins
sialic acids
Casein
C terminal peptide
Electrophoretic mobility
Genetic variant
Chemical composition
Glycosylation
Comparative study
ISSN:0958-6946, 1879-0143
On-line přístup:Získat plný text
Tagy: Přidat tag
Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!
Popis
Shrnutí:Bovine κ-caseins of single variant phenotype (AA and BB) and mixed phenotype (AA, BB and AB) were purified from milk and the corresponding κ-casein macropeptides prepared by chymosin hydrolysis. The macropeptides were characterized by PAGE, Mono Q- and reverse-phase HPLC. Chromatographic profiles showed marked differences between the monovariant macropeptides, attributable to differences in glycosylation. The B variant macropeptide was found to be more highly glycosylated than the A variant with an apparently greater number of oligo-saccharide chains per peptide unit and a higher level of sialylation. The analytical profiles for the mixed variant sample were a composite of those for the individual variants, all components being accounted for by one or other variant. It was concluded that while the overall extent of glycosylation may vary, there are consistent patterns of glycosylation for each variant.
Bibliografie:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
ISSN:0958-6946
1879-0143
DOI:10.1016/S0958-6946(96)00034-9