Godovac-Zimmermann J, Shaw D, Conti A, McKenzie H
Biol Chem Hoppe Seyler. 1987 Apr;368(4):427-33. doi: 10.1515/bchm3.1987.368.1.427.
The presence of two new alpha-lactalbumins has been demonstrated in the colostrum of a single mare (Equus caballus, Persian Arab). They have been designated equine alpha-lactalbumin B and C, and that isolated previously from the milk of Australian horses (English Thoroughbred) as alpha-lactalbumin A. The primary structures of B/C have been determined by automatic Edman degradation of enzymatic cleavage of the oxidized protein. Cyanogen bromide cleavage of S-carbamoyl-methylated protein provided necessary overlapping peptides. Comparison of the sequences of B and C with that of A indicates 3 and 4 amino-acid exchanges, respectively. The phylogenetic difference of equine alpha-lactalbumin B/C from bovine alpha-lactalbumin B is indicated by 39 and 40 amino-acid exchanges, respectively. The structure-function relationship, calcium binding sites and variants of alpha-lactalbumin are discussed.
在一匹母马（马属动物，波斯阿拉伯马）的初乳中发现了两种新的α-乳白蛋白。它们被命名为马α-乳白蛋白B和C，而之前从澳大利亚马（英国纯种马）的乳汁中分离出的被命名为α-乳白蛋白A。通过对氧化蛋白进行酶解后自动进行埃德曼降解法确定了B/C的一级结构。对S-氨甲酰甲基化蛋白进行溴化氰裂解得到了必要的重叠肽段。将B和C的序列与A的序列进行比较，结果表明分别有3个和4个氨基酸发生了交换。马α-乳白蛋白B/C与牛α-乳白蛋白B的系统发育差异分别由39个和40个氨基酸交换所表明。文中还讨论了α-乳白蛋白的结构-功能关系、钙结合位点及变体。
