从大鼠颌下腺分离出的两种激肽释放酶家族基因产物的底物特异性。

Substrate specificity of two kallikrein family gene products isolated from the rat submaxillary gland.

作者信息

Elmoujahed A, Gutman N, Brillard M, Gauthier F

机构信息

University François Rabelais, Faculty of Medicine, CNRS URA1334, Tours, France.

出版信息

FEBS Lett. 1990 Jun 4;265(1-2):137-40. doi: 10.1016/0014-5793(90)80903-v.

DOI:10.1016/0014-5793(90)80903-v

PMID:2194829

Abstract

Two proteinases which belong to the tissue kallikrein family were purified from rat submaxillary glands. These proteinases correspond to the products of the RSKG-7 and the rGK8 genes, as shown by the comparison of their partial amino-acid sequence with that deduced from nucleotide sequences. These two proteinases, kallikrein k7 and kallikrein k8, exhibit a marked preference for cleavage after arginyl residues. However, their overall specificities towards synthetic fluorogenic substrates differ significantly from each other and from that of true tissue kallikrein. Kallikrein k7 is strongly inhibited by soybean trypsin inhibitor, whereas kallikrein k8 is not. These data, demonstrating the individual specificity of these kallikrein-like proteinases, suggest that they could be involved in the processing of peptides other than kinins.

摘要

从大鼠颌下腺中纯化出两种属于组织激肽释放酶家族的蛋白酶。通过将它们的部分氨基酸序列与从核苷酸序列推导出来的序列进行比较，发现这些蛋白酶分别对应于RSKG-7和rGK8基因的产物。这两种蛋白酶，激肽释放酶k7和激肽释放酶k8，对精氨酰残基之后的切割表现出明显的偏好。然而，它们对合成荧光底物的总体特异性彼此之间以及与真正的组织激肽释放酶都有显著差异。激肽释放酶k7受到大豆胰蛋白酶抑制剂的强烈抑制，而激肽释放酶k8则不受抑制。这些数据证明了这些类激肽释放酶蛋白酶的个体特异性，表明它们可能参与除激肽之外的肽的加工过程。