Nisbet A D, Saundry R H, Moir A J, Fothergill L A, Fothergill J E
Eur J Biochem. 1981 Apr;115(2):335-45. doi: 10.1111/j.1432-1033.1981.tb05243.x.
The complete amino acid sequence of hen ovalbumin, comprising 385 residues, has been determined. The sequence was deduced from the 17 cyanogen bromide fragments and from peptides derived by digestion with a number of proteolytic enzymes. The molecular weight of the polypeptide chain of ovalbumin is 42699. Ovalbumin has four sites of postsynthetic modification; in addition to the acetylated N terminus, the carbohydrate moiety is located at Asn-292, and the two phosphorylated serines are at residues 68 and 344. The 'signal sequence' of ovalbumin is between residues 234 and 252. The heptapeptide released during the conversion of ovalbumin to plakalbumin by subtilisin digestion corresponds to residues 346-352. The hen ovalbumin polymorphism characterised by an Asn leads to Asp replacement results from a mutation at residue 311. The amino acid sequence of ovalbumin deduced from these amino acid sequence studies is in complete agreement with the sequence of mRNA determined by McReynolds et al. [Nature (Lond.) 273, 723-728 (1978)].
已确定含有385个残基的母鸡卵清蛋白的完整氨基酸序列。该序列是从17个溴化氰片段以及用多种蛋白水解酶消化产生的肽段推导出来的。卵清蛋白多肽链的分子量为42699。卵清蛋白有四个合成后修饰位点;除了N端乙酰化外,糖基部分位于Asn-292,两个磷酸化的丝氨酸分别位于第68位和第344位残基处。卵清蛋白的“信号序列”位于第234位和第252位残基之间。枯草杆菌蛋白酶消化使卵清蛋白转化为卵白蛋白过程中释放的七肽对应于第346 - 352位残基。以Asn突变为Asp为特征的母鸡卵清蛋白多态性是由第311位残基处的突变引起的。从这些氨基酸序列研究推导出来的卵清蛋白氨基酸序列与McReynolds等人[《自然》(伦敦)273, 723 - 728(1978)]测定的mRNA序列完全一致。