来自白纹伊蚊培养细胞的乳酸脱氢酶：动力学和同工酶分析。
Lactate dehydrogenase from cultured Aedes albopictus cells: kinetic and isozyme analysis.
作者信息
Torres-da Matta J, Silva C B, Hassón-Voloch A, Rebello M A
机构信息
Laboratório de Físico-Química Biológica, Universidade Federal do Rio de Janeiro.
出版信息
An Acad Bras Cienc. 1987;59(4):433-7.
L(+) lactate dehydrogenase (LDH) activity from cultured cells of Aedes albopictus was studied as a kinetic model of carbohydrate metabolism. Enzyme kinetics were studied in the forward (lactate as substrate) and reverse (pyruvate as substrate) reactions and the apparent Km values were obtained showing LDH higher affinity for pyruvate. The Hill coefficient values for each substrate were similar and indicate the existence of only one binding site on the enzyme. Isozyme analysis on cellulose-acetate electrophoresis presented a single band of LDH which presumably is of the LDH-5 type. The results obtained contribute to the assumption that Aedes albopictus cells have a predominance of anaerobic metabolism.
研究了白纹伊蚊培养细胞中的L(+)乳酸脱氢酶(LDH)活性，将其作为碳水化合物代谢的动力学模型。在正向反应(以乳酸为底物)和反向反应(以丙酮酸为底物)中研究了酶动力学，并获得了表观Km值，结果表明LDH对丙酮酸具有更高的亲和力。每种底物的希尔系数值相似，表明该酶上仅存在一个结合位点。醋酸纤维素电泳的同工酶分析显示LDH有一条单一的条带，推测为LDH-5型。所得结果支持了白纹伊蚊细胞主要进行无氧代谢的假设。
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