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在稀酸中天门冬氨酰-脯氨酰肽键处的优先裂解。

Preferential cleavage at aspartyl-prolyl peptide bonds in dilute acid.

作者信息

Marcus F

出版信息

Int J Pept Protein Res. 1985 May;25(5):542-6. doi: 10.1111/j.1399-3011.1985.tb02208.x.

DOI:10.1111/j.1399-3011.1985.tb02208.x
PMID:4019034
Abstract

A simple, rapid technique is presented for preferential cleavage at aspartylprolyl peptide bonds. The method is based upon the fact that these peptide bonds are 8-20-fold more labile in 0.015 N HCl at 100-110 degrees than other aspartyl-X or X-aspartyl peptide bonds. The method has proven effective in the cleavage of several peptides from pig kidney fructose-1,6-bisphosphatase and should facilitate sequence analysis of proteins that contain aspartyl-prolyl linkages.

摘要

本文介绍了一种在天冬氨酰-脯氨酰肽键处进行优先裂解的简单、快速技术。该方法基于这样一个事实，即这些肽键在100-110℃的0.015N盐酸中比其他天冬氨酰-X或X-天冬氨酰肽键更不稳定8-20倍。该方法已被证明对从猪肾果糖-1,6-二磷酸酶中裂解几种肽有效，并且应该有助于对含有天冬氨酰-脯氨酰连接的蛋白质进行序列分析。

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