人血红蛋白α链104位半胱氨酸处的特异性氰化及裂解。“指纹”法研究血红蛋白变异体时α链胰蛋白酶核心问题的一种新方法。
Specific cyanylation and cleavage at cysteine-104 human hemoglobin alpha-chain. A novel approach to the problem of the alpha-chain tryptic core in the study of haemoglobin variants by "fingerprinting" methods.
作者信息
Casey R, Lang A
出版信息
Biochem J. 1975 Feb;145(2):251-61. doi: 10.1042/bj1450251.
Abstract
- A new approach to the analysis, by "fingerprinting", of the tryptic core region of human haemoglobin alpha-chain is described. 2. The alpha-chain is cyanylated at its single cysteine residue (alpha104) and then split, by exposure to mild alkali, at the N-peptide bond of the resulting beta-thiocyanoalanine residue. 3. The two cleavage fragments, alpha1-103 and alpha104-141, are separated by gel filtration, and the fragment alpha104-141, which contains all the residues of the alpha-chain tryptic core, is digested with pepsin. 4. Preparative "fingerprints" of these peptic peptides yield eight major peptides, which provide complete sequence information for the whole region alpha104-141. 5. The utility of the method is demonstrated by repeating the determination of the substitution in haemoglobin Hopkins-2, a known alpha-chain core variant in which histidine-alpha112 (G19) is replaced by an aspartic acid residue.
摘要
- 本文描述了一种通过“指纹图谱”分析人血红蛋白α链胰蛋白酶核心区域的新方法。2. α链在其单个半胱氨酸残基（α104）处进行氰化，然后通过暴露于弱碱，在所得β-硫氰基丙氨酸残基的N-肽键处裂解。3. 通过凝胶过滤分离两个裂解片段α1-103和α104-141，并且用胃蛋白酶消化包含α链胰蛋白酶核心所有残基的片段α104-141。4. 这些胃蛋白酶肽段的制备性“指纹图谱”产生八个主要肽段，它们提供了整个α104-141区域的完整序列信息。5. 通过重复测定血红蛋白霍普金斯-2中的取代来证明该方法的实用性，血红蛋白霍普金斯-2是一种已知的α链核心变体，其中组氨酸-α112（G19）被天冬氨酸残基取代。
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