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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.

作者信息

Corran P H, Waley S G

出版信息

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

Abstract
  1. 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
  1. 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。

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Structural studies on bovine -crystallin.牛β-晶状体蛋白的结构研究。
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Structural studies on lens proteins.晶状体蛋白的结构研究。
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Structural studies of alpha-crystallin.α-晶状体蛋白的结构研究。
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N-terminal sequences of alpha-crystallin.α-晶状体蛋白的N端序列
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本文引用的文献

1
PREFERENTIAL RELEASE OF ASPARTIC ACID BY DILUTE ACID TREATMENT OF TRYPTIC PEPTIDES.
Biochemistry. 1965 May;4:793-801. doi: 10.1021/bi00881a001.
3
Splitting and recombination of alpha-crystallin.α-晶状体蛋白的分裂与重组
Exp Eye Res. 1962 Jun;1:300-5. doi: 10.1016/s0014-4835(62)80015-3.
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The action of trypsin on polylysine.胰蛋白酶对聚赖氨酸的作用。
Biochem J. 1953 Sep;55(2):328-37. doi: 10.1042/bj0550328.
5
Structural studies on lens proteins.晶状体蛋白的结构研究。
Biochem J. 1967 Jul;104(1):128-34. doi: 10.1042/bj1040128.
8
Structural studies of alpha-crystallin.α-晶状体蛋白的结构研究。
Biochem J. 1965 Sep;96(3):722-8. doi: 10.1042/bj0960722.
10
Molecular weight determination from amino acid analysis data: a numerical method.
Anal Biochem. 1968 Oct 24;25(1):417-31. doi: 10.1016/0003-2697(68)90117-6.

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