小牛晶状体β-晶状体蛋白半胱氨酸残基周围的氨基酸序列。

Amino acid sequences around the cysteine residue of calf lens -crystallin.

Corran P H, Waley S G

Biochem J. 1971 Aug;124(1):61-7. doi: 10.1042/bj1240061.

Abstract

Calf lens alpha-crystallin was carboxymethylated with radioactive sodium iodoacetate to label the thiol group. 2. The protein was then digested with trypsin or alternatively fractionated in urea to obtain the acidic (A) chains, which were then digested with trypsin. Either procedure gave two radioactive peptides containing carboxymethylcysteine. 3. These two peptides were closely related: the longer form contained 28 amino acid residues, and the shorter lacked two residues at the N-terminal end of the longer form. 4. The amino acid sequence of the peptides have been determined. 5. No evidence for the presence of more than one cysteine residue/chain was found. 6. The question of the molecular weight of the chains is discussed.

摘要

用放射性碘乙酸钠对小牛晶状体α-晶状体蛋白进行羧甲基化，以标记巯基。2. 然后用胰蛋白酶消化该蛋白质，或者在尿素中进行分级分离以获得酸性（A）链，随后用胰蛋白酶消化这些链。这两种方法都得到了两条含有羧甲基半胱氨酸的放射性肽段。3. 这两条肽段密切相关：较长的形式含有28个氨基酸残基，较短的形式在较长形式的N末端缺少两个残基。4. 已经确定了这些肽段的氨基酸序列。5. 未发现每条链存在一个以上半胱氨酸残基的证据。6. 讨论了这些链的分子量问题。