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人类多形核白细胞氨肽酶

Human polymorphonuclear leukocytes aminopeptidases.

作者信息

Vitale L, Grdisa M, Wrischer M

出版信息

Folia Histochem Cytobiol. 1986;24(2):139-48.

PMID:3095153
Abstract

In human polymorphonuclear leukocytes a methionine, leucine, arginine, phenylalanine and alanine aminopeptidase activities were detected, both in cytosol and secondary granules. All activities were EDTA sensitive and their pH optima were in the range of pH 6.5 to 8.6. In the cytosol two enzymes could be distinguished, broad substrate specificity aminopeptidase of pH 4.7-4.9 and a chloride dependent arginine aminopeptidase of pI 5.3-5.5. The granules contain aminopeptidase of pI 4.0-4.6 and of pI 9.8-10.2, different from those in the cytosol. Among them broad specificity aminopeptidases and possibly specific methionine and leucine aminopeptidases could be discerned.

摘要

在人类多形核白细胞中,在胞质溶胶和次级颗粒中均检测到甲硫氨酸、亮氨酸、精氨酸、苯丙氨酸和丙氨酸氨肽酶活性。所有活性均对乙二胺四乙酸(EDTA)敏感,其最适pH值在6.5至8.6范围内。在胞质溶胶中可区分出两种酶,pH值为4.7 - 4.9的具有广泛底物特异性的氨肽酶和等电点(pI)为5.3 - 5.5的依赖氯化物的精氨酸氨肽酶。颗粒中含有等电点为4.0 - 4.6和9.8 - 10.2的氨肽酶,与胞质溶胶中的不同。其中可识别出具有广泛特异性的氨肽酶以及可能特定的甲硫氨酸和亮氨酸氨肽酶。

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