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α2巨球蛋白在囊性纤维化中与蛋白酶的结合

Protease binding by alpha 2 macroglobulin in cystic fibrosis.

作者信息

Bridges M A, Applegarth D A, Johannson J, Wong L T, Davidson A G

出版信息

Clin Chim Acta. 1982 Jan 5;118(1):33-43. doi: 10.1016/0009-8981(82)90224-8.

Abstract

The interaction of alpha 2 macroglobulin (alpha 2M) with exogenous proteases has been reported by others to be abnormal in cystic fibrosis (CF). We have re-examined these claims. Four parameters were considered:(1) the molar protease binding of alpha 2M; (2) the interaction of bovine cationic trypsin (BCT), complexed to alpha 2M, with low molecular mass substrate, benzoyl arginine ethyl ester (BAEE); (3) the stability of formed alpha 2 M-BCT complexes; and (4) the subunit structure of alpha 2M. We have found CF alpha 2M to be similar to control alpha 2M in every respect studied.

摘要

其他人已报道α2巨球蛋白(α2M)与外源性蛋白酶的相互作用在囊性纤维化(CF)中异常。我们重新审视了这些说法。考虑了四个参数:(1)α2M的摩尔蛋白酶结合;(2)与α2M复合的牛阳离子胰蛋白酶(BCT)与低分子量底物苯甲酰精氨酸乙酯(BAEE)的相互作用;(3)形成的α2M - BCT复合物的稳定性;以及(4)α2M的亚基结构。我们发现在所研究的各个方面,CFα2M与对照α2M相似。

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