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青霉胃蛋白酶的氨基酸序列。II. 热解肽的分离与特性鉴定

Amino acid sequence of penicillopepsin. II. Isolation and characterization of thermolytic peptides.

作者信息

Rao L, Hofmann T

出版信息

Can J Biochem. 1976 Oct;54(10):885-94. doi: 10.1139/o76-126.

Abstract

The determination of the amino acid sequences of 70 peptides obtained from a thermolytic digest of penicillopepsin (EC 3.4.23.7) is described. Fifty-six unique sequences ranging from 2 to 13 amino acids were compiled. Among these was a heptapeptide whose sequence is nearly identical with that of the epoxide-reactive active site peptide of porcine pepsin (EC 3.4.23.1). Considering unrecognized overlaps, a minimum of 272 and a maximum of 293 unique amino acids have been obtained. They account for about 90% of the amino acids of the enzyme.

摘要

本文描述了从青霉胃蛋白酶(EC 3.4.23.7)的热解消化产物中获得的70个肽段的氨基酸序列测定结果。共汇编了56个独特序列,长度从2到13个氨基酸不等。其中有一个七肽,其序列与猪胃蛋白酶(EC 3.4.23.1)的环氧化物反应活性位点肽的序列几乎相同。考虑到未识别的重叠情况,已获得最少272个和最多293个独特氨基酸。它们约占该酶氨基酸的90%。

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