来自荞麦种子的阴离子蛋白酶抑制剂BWI-1。动力学特性及可能的生物学作用。

The anionic protease inhibitor BWI-1 from buckwheat seeds. Kinetic properties and possible biological role.

作者信息

Dunaevsky Yakov E, Gladysheva Inna P, Pavlukova Ekaterina B, Beliakova Galina A, Gladyshev Dmitry P, Papisova Alla I, Larionova Natalja I, Belozersky Mikhail A

机构信息

A. N. Belozersky Inst. of Physico-Chemical Biology.

Dept of Chemistry, Moscow State Univ., Moscow 119899, Russia.

出版信息

Physiol Plant. 1997 Nov;101(3):483-488. doi: 10.1111/j.1399-3054.1997.tb01027.x.

DOI:10.1111/j.1399-3054.1997.tb01027.x

PMID:37340607

Abstract

Kinetic characteristics and effects on the growth of filamentous fungi of one of the main anionic protease inhibitors, BWI-1, isolated from buckwheat seeds, have been studied. The inhibition constants of bovine trypsin, chymotrypsin and cathepsin G from human granulocytes with BWI-1 were found to be 1.1, 67 and 200 nM, respectively. Analysis of the amino acid sequence of BWI-1 in the vicinity of the reactive site revealed its homology to the potato proteinase inhibitor I family. It is suggested that the inability of BWI-1 to bind elastase of human granulocytes is due to the basic nature of the amino acid residue (Arg) at the P position in its reactive site. It was demonstrated that BWI-1 was able to suppress the germination of the spores and the growth of the mycelium of two filamentous fungi.

摘要

对从荞麦种子中分离出的一种主要阴离子蛋白酶抑制剂BWI-1的动力学特性及其对丝状真菌生长的影响进行了研究。发现BWI-1对牛胰蛋白酶、胰凝乳蛋白酶和人粒细胞组织蛋白酶G的抑制常数分别为1.1、67和200 nM。对BWI-1活性位点附近的氨基酸序列分析表明，它与马铃薯蛋白酶抑制剂I家族具有同源性。有人认为，BWI-1不能与人粒细胞弹性蛋白酶结合是由于其活性位点P位置的氨基酸残基（Arg）具有碱性。结果表明，BWI-1能够抑制两种丝状真菌的孢子萌发和菌丝生长。