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- W2022091126 abstract "SUMMARY The primary structures of ovine α >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 ∼ 80% of the entire translated αsl-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 αsl-casein A, whereas Ser 115 and Ser 41 were phosphorylated by ∼ 50 and ∼ 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 Ser 13 →> Pro 13 which determined the loss of the phosphate group on site 12 of the protein chain, SerP 12 →>Ser 12 . A further substitution, SerP 68 →> Asn 68 caused the disappearance of both phosphate groups in the phosphorylated residues Ser 64 and Ser 66 in variant D; in this last casein variant there was no evidence of phosphorylation at Ser 41 ." @default.
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- W2022091126 date "1995-05-01" @default.
- W2022091126 modified "2023-09-27" @default.
- W2022091126 title "Primary structure of ovine α<sub>sl</sub>-caseins: localization of phosphorylation sites and characterization of genetic variants A, C and D" @default.
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- W2022091126 doi "https://doi.org/10.1017/s0022029900030983" @default.
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