关联酶活性分析的新关系
New relations for activity analysis of associating enzymes.
作者信息
Thomes J C, Archambault De Vençay J, Julien R
出版信息
Biochem J. 1980 Feb 1;185(2):339-47. doi: 10.1042/bj1850339.
Abstract
New relations for catalytic-activity analysis are proposed for simple association/dissociation equilibria between the mono- and oligo-meric forms of enzymes in the case where these equilibria evolve very slowly in comparison with the binding of the substrates. This analysis of activity versus total enzyme concentration leads rapidly to information, complementary to that given by physico-chemical methods, on specific activities, the degree of polymerization of the enzyme forms and on their dissociation constants.
摘要
对于酶的单体和寡聚体形式之间的简单缔合/解离平衡，在这些平衡相对于底物结合而言演化非常缓慢的情况下，提出了用于催化活性分析的新关系。这种活性与总酶浓度的分析能够迅速得出与物理化学方法所提供信息互补的信息，这些信息涉及比活性、酶形式的聚合度及其解离常数。
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