CYANYLATION OF SULFHYDRYL GROUPS BY 2-NITRO-5-THIOCYANOBENZOIC ACID - HIGH-YIELD MODIFICATION AND CLEAVAGE OF PEPTIDES AT CYSTEINE RESIDUES
CYANYLATION OF SULFHYDRYL GROUPS BY 2-NITRO-5-THIOCYANOBENZOIC ACID - HIGH-YIELD MODIFICATION AND CLEAVAGE OF PEPTIDES AT CYSTEINE RESIDUES
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DOI：
10.1021/bi00698a001
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发表时间：
1974-01-01
期刊：
影响因子：
2.9
通讯作者：
PATCHORNIK, A
中科院分区：
文献类型：
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作者：
DEGANI, Y;PATCHORNIK, A
Y. Degani** 和 A. Patchornik 摘要：使用稀溶液中的试剂 2-硝基-5-硫氰基-苯甲酸对含有半胱氨酸残基的肽进行定量 S-氰基化。随着反应物浓度的增加，氰基化程度降低，并形成可识别的副产物。动力学研究表明，这些副产物是由一系列浓度依赖性连续竞争反应产生的，这些反应是由试剂与其释放的离去基团之间的相互作用引发的。通过修饰获得的放射性标记/3-硫氰基丙氨酸肽，通过在 37-50、pH 8 下孵育，在修饰残基的 N-肽键处以高产率裂解，形成 2-亚氨基噻唑烷
Y. Degani** and A. Patchornik abstract: Peptides containing cysteine residues were quantitatively S-cyanylated using thereagent 2-nitro-5-thiocyano-benzoic acid in dilute solutions. With increasing concentra-tions of the reactants, the extent of cyanylation decreased, and identifiable side products were formed. Kinetic studies in-dicated that these side products resulted from a series of con-centration-dependent consecutive competitive reactions, ini-tiated by an interaction between the reagent and its released leaving group. Radioactively labeled/3-thiocyanoalanine peptides obtained by the modification, were cleaved in high yields at the N-peptide bond of the modified residue, by in-cubations at 37-50 at pH 8, to form 2-iminothiazolidine