激肽原作为硫醇蛋白酶抑制剂的新功能：牛、大鼠和人血浆激肽原对木瓜蛋白酶和组织蛋白酶B、H及L的抑制作用

A new function of kininogens as thiol-proteinase inhibitors: inhibition of papain and cathepsins B, H and L by bovine, rat and human plasma kininogens.

作者信息

Sueyoshi T, Enjyoji K, Shimada T, Kato H, Iwanaga S, Bando Y, Kominami E, Katunuma N

出版信息

FEBS Lett. 1985 Mar 11;182(1):193-5. doi: 10.1016/0014-5793(85)81182-0.

Abstract

The amidolytic activities of papain and rat liver cathepsins B, H and L were strongly inhibited by high (HMM) and low (LMM) molecular mass kininogens from bovine, human and rat plasmas, and their Ki values were estimated to be in the order of 10(-10) - 10(-11)M for papain and 10(-8) - 10(-9)M for cathepsins. The derivatives of bovine kininogens, HMM kinin-free protein, HMM kinin- and fragment 1 X 2-free protein, and LMM kinin-free protein also showed strong inhibitory activity toward these thiol-proteinases. These results suggest that a reactive site which interacts with thiol-proteinases is contained in the heavy chain portion in kininogens.

摘要

木瓜蛋白酶以及大鼠肝脏组织蛋白酶B、H和L的酰胺水解活性受到来自牛、人及大鼠血浆的高分子量（HMM）和低分子量（LMM）激肽原的强烈抑制，木瓜蛋白酶的Ki值估计在10⁻¹⁰ - 10⁻¹¹M范围内，组织蛋白酶的Ki值在10⁻⁸ - 10⁻⁹M范围内。牛激肽原的衍生物，即无HMM激肽的蛋白、无HMM激肽和1X2片段的蛋白以及无LMM激肽的蛋白，对这些巯基蛋白酶也表现出强烈的抑制活性。这些结果表明，激肽原重链部分含有与巯基蛋白酶相互作用的反应位点。