通过色谱聚焦分析的A类β-内酰胺酶的参差不齐的N端及其他变体。
Ragged N-termini and other variants of class A beta-lactamases analysed by chromatofocusing.
作者信息
Matagne A, Joris B, Van Beeumen J, Frère J M
机构信息
Laboratoire d'Enzymologie, Université de Liège, Sart Tilman, Belgium.
出版信息
Biochem J. 1991 Feb 1;273 ( Pt 3)(Pt 3):503-10. doi: 10.1042/bj2730503.
Abstract
Four beta-lactamases excreted by Gram-positive bacteria exhibited microheterogeneity when analysed by chromatofocusing or ion-exchange chromatography. Ragged N-termini were in part responsible for the charge variants, but deamidation of an asparagine residue was also involved, at least for the Bacillus licheniformis enzyme. The activity of a contaminating proteinase could also be demonstrated in the case of Actinomadura R39 beta-lactamase. With that enzyme, proteolysis resulted in partial inactivation, but the inactivated fragments were easily separated from the active forms. With these, as with the other enzymes, the kinetic parameters of the major variants were identical with those of the mixture within the limits of experimental error, so that the catalytic properties of these enzymes can be determined with the 'heterogeneous' preparations.
摘要
革兰氏阳性菌分泌的四种β-内酰胺酶经色谱聚焦或离子交换色谱分析时呈现出微不均一性。参差不齐的N端部分导致了电荷变体的产生，但天冬酰胺残基的脱酰胺作用也参与其中，至少对于地衣芽孢杆菌的酶是这样。在马杜拉放线菌R39β-内酰胺酶的情况下，也能证明一种污染性蛋白酶的活性。对于该酶，蛋白水解导致部分失活，但失活片段很容易与活性形式分离。对于这些酶以及其他酶，在实验误差范围内，主要变体的动力学参数与混合物的动力学参数相同，因此可以用“不均一”制剂来确定这些酶的催化特性。
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