通过酶固定化或抑制消除自噬变性。

Elimination of cannibalistic denaturation by enzyme immobilization or inhibition.

机构信息

Department of Chemistry, Northwestern University, Evanston, Illinois 60201.

出版信息

Proc Natl Acad Sci U S A. 1981 Jul;78(7):4118-9. doi: 10.1073/pnas.78.7.4118.

DOI:10.1073/pnas.78.7.4118

PMID:16593052

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC319738/

Abstract

The cannibalistic denaturation of alpha-chymotrypsin (EC 3.4.21.1) around neutral pH can be eliminated by immobilization (insolubilization) of the enzyme or by inhibition by specific reversible inhibitors, but the high-pH denaturation cannot be. The denaturation of the immobilized enzyme at high pH follows first-order kinetics, just as the denaturation of the soluble enzyme does. These results lend credence to the description of the denaturation of chymotrypsin as cannibalistic around neutrality and due to a hydroxide ion reaction at high pH; this interpretation followed from kinetic arguments given in the previous article [Wu, H.-L., Wastell, A. & Bender, M. L. (1981) Proc. Natl. Acad. Sci. USA 78, 4116-4117]. Elimination of denaturation around neutrality by immobilization may be the reason why membrane-bound enzymes are so common in vivo.

摘要

中性 pH 环境下，糜蛋白酶（EC 3.4.21.1）的自噬变性可以通过酶的固定化（不溶）或特定可逆抑制剂的抑制来消除，但不能消除高 pH 下的变性。在高 pH 下，固定化酶的变性遵循一级反应动力学，就像可溶性酶的变性一样。这些结果为糜蛋白酶在中性附近的自噬变性以及在高 pH 下由于氢氧离子反应的描述提供了依据；这一解释源于前文 [Wu, H.-L., Wastell, A. & Bender, M. L. (1981) Proc. Natl. Acad. Sci. USA 78, 4116-4117] 中的动力学论据。通过固定化消除中性附近的变性可能是膜结合酶在体内如此普遍的原因。