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.
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机译:Walker,Hazel(格鲁吉亚大学,雅典)和R. G. Eagon。 假单胞菌的乳酸脱氢酶 em>。 J. Bacteriol。 > 88: strong> 25-30。 1964年。在假单胞菌 EM>中,证明了对D-和L-乳酸特异的乳酸脱氢酶。 L-乳酸脱氢酶显示出相当大的热稳定性,并且在60℃加热10分钟后,在提取物中仍然存在40%的活性。注意到酶活性的必需硫醇组。这些实验的结果与乳酸盐最初通过黄素辅因子脱氢的视野一致,并且将电子通过完全末端氧化酶系统转运至氧气。将这些乳酸脱氢酶的细胞内部位显示为细胞膜。建议这些乳酸脱氢酶的主要生理作用是乳酸利用的主要生理作用。
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