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嗜盐假单胞菌的乳酸脱氢酶

LACTIC DEHYDROGENASES OF PSEUDOMONAS NATRIEGENS.

作者信息

WALKER H, EAGON R G

出版信息

J Bacteriol. 1964 Jul;88(1):25-30. doi: 10.1128/jb.88.1.25-30.1964.

Abstract

Walker, Hazel (University of Georgia, Athens), and R. G. Eagon. Lactic dehydrogenases of Pseudomonas natriegens. J. Bacteriol. 88:25-30. 1964.-Lactic dehydrogenases specific for d- and l-lactate were demonstrated in Pseudomonas natriegens. The l-lactic dehydrogenase showed considerable heat stability, and 40% of the activity remained in extracts after heating at 60 C for 10 min. An essential thiol group for enzyme activity was noted. The results of these experiments were consistent with the view that lactate was dehydrogenated initially by a flavin cofactor and that electrons were transported through a complete terminal oxidase system to oxygen. The intracellular site of these lactic dehydrogenases was shown to be the cell membrane. It was suggested that the main physiological role of these lactic dehydrogenases is that of lactate utilization.

摘要

沃克,黑兹尔(佐治亚大学,雅典),以及R. G. 伊根。产气假单胞菌的乳酸脱氢酶。《细菌学杂志》88:25 - 30。1964年。——在产气假单胞菌中证实了对d - 乳酸和l - 乳酸具有特异性的乳酸脱氢酶。l - 乳酸脱氢酶表现出相当高的热稳定性,在60℃加热10分钟后,提取物中仍保留40%的活性。发现了酶活性所必需的巯基。这些实验结果与以下观点一致,即乳酸最初由黄素辅因子脱氢,电子通过完整的末端氧化酶系统传递给氧气。这些乳酸脱氢酶的细胞内定位显示为细胞膜。有人提出这些乳酸脱氢酶的主要生理作用是乳酸利用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/096d/277251/d568c0f78715/jbacter00436-0056-a.jpg

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