磷酸化
序列(生物学)
肽序列
鉴定(生物学)
酪蛋白
BETA(编程语言)
生物化学
化学
氨基酸
计算生物学
生物
计算机科学
基因
植物
程序设计语言
作者
Rae Greenberg,M.L. Groves,Harold J. Dower
标识
DOI:10.1016/s0021-9258(17)42966-8
摘要
The primary structure of human beta-casein has been determined by automated Edman degradation of the intact protein and of peptides derived therefrom by hydrolysis with trypsin and by chemical cleavage with cyanogen bromide. For each form of this multiphosphorylated protein (0-5 P/molecule), phosphorylated sites at specific seryl and threonyl residues have been identified. These are located near the amino terminus, within the first 10 residues of this 212-amino acid molecule. Sequence comparison of human beta-casein with the bovine and ovine proteins reveals 50% identity and a 10-residue shifted alignment relationship. Locations of prolyl and charged residues are generally conserved for the three homologues. The sequence data indicate the existence of genetic polymorphism involving uncharged residues in human beta-casein.
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