Biochemical characterization of the bovine genetic kappa-casein C and E variants.
Analysis of elution profiles of enzymatic and CNBr digests of kappa-caseins C and E, and sequencing of most relevant peptides allowed the chemical characterization of both genetic variants. They differ from their B and A allelic counterparts by a single substitution, His97/Arg and Gly155/Ser, respectively. Electrophoretic behaviour of the investigated C and E variants was in good agreement with the observed amino acid replacements.
Station de Recherches Laitières, INRA CRJ, Jouy-en-Josas, France.
G
G
Miranda
P
P
Anglade
M F
MF
Mahé
G
G
Erhardt
D000483:Alleles; D000595:Amino Acid Sequence; D000818:Animals; D002364:Caseins / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D002417:Cattle / Q000235:genetics*; D002851:Chromatography, High Pressure Liquid / Q000662:veterinary; D004592:Electrophoresis, Starch Gel / Q000662:veterinary; D014644:Genetic Variation; D007525:Isoelectric Focusing / Q000662:veterinary; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics*; D010449:Peptide Mapping / Q000662:veterinary; D017354:Point Mutation; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid
D002364:Caseins; D010446:Peptide Fragments