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

Preferential cleavage at aspartyl-prolyl peptide bonds in dilute acid.
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在稀酸中优先裂解天冬氨酰-脯氨酰肽键。

DOI:
10.1111/j.1399-3011.1985.tb02208.x
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发表时间:
1985
期刊:
International journal of peptide and protein research
影响因子:
--
通讯作者:
Marcus,F
Marcus,F
中科院分区:
--
文献类型:
--
作者:
Marcus,F

文献摘要

被引文献

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提出了一种简单、快速的技术来优先切割天冬氨酰-脯氨酰肽键。该方法基于以下事实:在100-110° C下,这些肽键在0.015 nHCl中的不稳定性是其他乙酰基-X或X-乙酰基肽键的8-20倍。该方法已被证明可有效切割猪肾果糖-1,6-二磷酸酶中的几种肽,并应有助于含有乙酰-脯氨酰键的蛋白质的序列分析。
A simple, rapid technique is presented for preferential cleavage at aspartyl‐prolyl peptide bonds. The method is based upon the fact that these peptide bonds are 8–20‐fold more labile in 0.015nHCl at 100–110° 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.