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大鼠颌下腺激肽释放酶k10(激肽释放酶家族成员之一)的微观异质性

Microheterogeneity of rat submaxillary gland kallikrein k10, a member of the kallikrein family.

作者信息

Gutman N, Elmoujahed A, Brillard M, Du Sorbier B M, Gauthier F

机构信息

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

出版信息

Eur J Biochem. 1991 Apr 23;197(2):425-9. doi: 10.1111/j.1432-1033.1991.tb15928.x.

DOI:10.1111/j.1432-1033.1991.tb15928.x
PMID:2026164
Abstract

A tissue-kallikrein-related proteinase present in rat submaxillary glands, which was previously called endopeptidase k, has been further characterized and compared with other members of the kallikrein family. The partial primary structure of this proteinase, now called kallikrein k10, is very similar to that of proteinase B [Kato, H., Nakanishi, E., Enjyoji, K., Hayashi, I., Oh-Ishi, S. & Iwanaga, S. (1987) J. Biochem. (Tokyo) 102, 1389-1404] and T-kininogenase [Xiong, W., Chen. L. M. & Chao, J. (1990) J. Biol. Chem. 265, 2822-2827], but no corresponding gene or mRNA has so far been found. Kallikrein k10 is microheterogeneous due to variable glycosylation of its N-terminal light chain and to variable processing at its kallikrein loop, as shown by endo-beta-N-acetylglucosaminidase F treatment, amino acid sequence analysis and mass spectrometry. The enzymatic properties of the two molecular varieties of kallikrein k10 towards synthetic fluorogenic substrates are not significantly different. Both cleave specifically after Arg residues, but, in contrast to true tissue kallikrein, may accommodate either polar or nonpolar residues at position P2. Kallikrein k10 also differs from tissue kallikrein by its sensitivity to soyabean trypsin inhibitor. Its biological function may therefore differ from that of tissue kallikrein, especially as it does not induce a transient decrease in blood pressure when injected in vivo.

摘要

一种存在于大鼠颌下腺中的组织激肽释放酶相关蛋白酶,之前被称为内肽酶k,现已得到进一步表征,并与激肽释放酶家族的其他成员进行了比较。这种蛋白酶(现称为激肽释放酶k10)的部分一级结构与蛋白酶B [加藤浩、中谷英二、远藤寺克、林一、大市史和岩永幸(1987年)《生物化学杂志》(东京)102卷,第1389 - 1404页]和T - 激肽原酶[熊伟、陈立民和赵军(1990年)《生物化学杂志》265卷,第2822 - 2827页]非常相似,但迄今为止尚未发现相应的基因或信使核糖核酸。如经内切β - N - 乙酰葡糖胺酶F处理、氨基酸序列分析和质谱分析所示,激肽释放酶k10由于其N端轻链的可变糖基化以及在激肽释放酶环处的可变加工而具有微异质性。激肽释放酶k10的两种分子变体对合成荧光底物的酶学性质没有显著差异。两者都特异性地在精氨酸残基之后切割,但与真正的组织激肽释放酶不同,在P2位置可以容纳极性或非极性残基。激肽释放酶k10对大豆胰蛋白酶抑制剂的敏感性也与组织激肽释放酶不同。因此,其生物学功能可能与组织激肽释放酶不同,尤其是在体内注射时它不会引起血压的短暂下降。

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Microheterogeneity of rat submaxillary gland kallikrein k10, a member of the kallikrein family.大鼠颌下腺激肽释放酶k10(激肽释放酶家族成员之一)的微观异质性
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Characterization of a new kallikrein-like enzyme (KLP-S3) of the rat submandibular gland.大鼠下颌下腺一种新的激肽释放酶样酶(KLP-S3)的特性研究。
Biochem J. 1992 Feb 1;281 ( Pt 3)(Pt 3):819-28. doi: 10.1042/bj2810819.