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N群链球菌中烟酰胺腺嘌呤二核苷酸依赖性D-和L-乳酸脱氢酶的纯化及性质

Purification and properties of nicotinamide adenine dinucleotide-dependent D- and L- lactate dehydrogenases in a group N streptococcus.

作者信息

Mou L, Mulvena D P, Jonas H A, Jago G R

出版信息

J Bacteriol. 1972 Aug;111(2):392-6. doi: 10.1128/jb.111.2.392-396.1972.

Abstract

Streptococcus lactis strain 760, a group N streptococcus, was found to possess nicotinamide adenine dinucleotide-dependent dehydrogenase activities for both the l(+) and the d(-) isomers of lactic acid. The two enzymes were isolated and purified and were found to differ with respect to pH optima, activation by fructose-1,6-diphosphate, pH and heat stability, and the temperature at which each enzyme was formed in the organism during growth. The presence of a racemase for lactic acid was not detected by the methods used.

摘要

乳酸链球菌760株,一种N群链球菌,被发现对乳酸的L(+)和D(-)异构体均具有烟酰胺腺嘌呤二核苷酸依赖性脱氢酶活性。两种酶被分离纯化,发现它们在最适pH值、1,6-二磷酸果糖的激活作用、pH值和热稳定性以及生长过程中每种酶在生物体中形成的温度方面存在差异。所使用的方法未检测到乳酸消旋酶的存在。

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本文引用的文献

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Protein measurement with the Folin phenol reagent.
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FRUCTOSE-1,6-DIPHOSPHATE REQUIREMENT OF STREPTOCOCCAL LACTIC DEHYDROGENASES.
Science. 1964 Nov 6;146(3645):775-7. doi: 10.1126/science.146.3645.775.
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Construction of a laboratory press for use with the French pressure cell.
Appl Microbiol. 1970 May;19(5):875-7. doi: 10.1128/am.19.5.875-877.1970.

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