SUSCEPTIBILITY OF NEUROACTIVE PEPTIDES TO AMINOPEPTIDASE DIGESTION IS RELATED TO MOLECULAR-SIZE

被引：21

作者：

AUSTEN, BM

EVANS, CJ

SMYTH, DG

机构：

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 91卷 / 04期

关键词：

D O I：

10.1016/0006-291X(79)91196-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Peptide fragments derived from the NH2-terminus of corticotropin were found to exhibit widely differing degrees of stability to degradation by aminopeptidase M. Corticotropin itself was 135 times more stable than its NH2-terminal pentapeptide, and similar differences in stability were observed with peptides derived from the B-chain of bovine insulin. Enkephalin linked covalently to the A-chain of bovine insulin was at least 100 times more stable than the pentapeptide. The results demonstrate that the molecular size of a peptide is one factor that determines its NH2-terminal stability. © 1979.

引用

页码：1211 / 1217

页数：7

共 15 条

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