牛β-晶状体蛋白的结构研究。
Structural studies on bovine -crystallin.
作者信息
Croft L R, Waley S G
出版信息
Biochem J. 1971 Feb;121(3):453-9. doi: 10.1042/bj1210453.
Abstract
The amino acid sequences around the cysteine residues in the lens protein, gamma-crystallin, were studied. Fraction II of the gamma-crystallin from calf lens (Björk, 1964) was used. The protein was oxidized with performic acid and then hydrolysed with trypsin. Six peptides containing cysteic acid were isolated. One of the peptides contained three residues of cysteic acid and the others contained one residue of cysteic acid. We conclude that there are eight unique residues of cysteic acid in the oxidized protein. Amino acid analysis suggests that there are also eight residues of cysteic acid in the molecule, which thus contains only one polypeptide chain.
摘要
对晶状体蛋白γ-晶体蛋白中半胱氨酸残基周围的氨基酸序列进行了研究。使用了来自小牛晶状体的γ-晶体蛋白的组分II（比约克，1964年）。该蛋白质先用过甲酸氧化，然后用胰蛋白酶水解。分离出了六种含半胱磺酸的肽。其中一种肽含有三个半胱磺酸残基，其他肽含有一个半胱磺酸残基。我们得出结论，氧化后的蛋白质中有八个独特的半胱磺酸残基。氨基酸分析表明，该分子中也有八个半胱磺酸残基，因此它只包含一条多肽链。
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