来自伯氏疟原虫的葡萄糖-6-磷酸脱氢酶：动力学和电泳特性

Glucose-6-phosphate dehydrogenase from Plasmodium berghei: kinetic and electrophoretic characterization.

作者信息

Buckwitz D, Jacobasch G, Kuckelkorn U, Megow D

机构信息

Institute of Biochemistry, School of Medicine (Charité), Humboldt-University, Berlin, G.D.R.

出版信息

Biomed Biochim Acta. 1990;49(2-3):S295-300.

PMID:2201291

Abstract

Evidence is given for the existence of a parasite-specific glucose-6-phosphate dehydrogenase in Plasmodium berghei by characterization of its kinetic and electrophoretic properties. After separating the parasites from infected RBC the G6PD was purified by affinity chromatography with 2'5'-ADP-Sepharose 4B. In cellulose acetate electrophoresis malarial G6PD significantly differs from the red cell enzyme. The subunits of the parasite-specific G6PD have a molecular weight of 55 kD in contrast to 59 kD of the RBC enzyme. G6PD from P. berghei shows no cross-reactivity with antibodies against G6PD from rat erythrocytes. The Km-value for G6P of malarial G6PD is increased by one order of magnitude compared with the host cell enzyme.

摘要

通过对伯氏疟原虫中寄生虫特异性葡萄糖-6-磷酸脱氢酶的动力学和电泳特性进行表征，证明了该酶的存在。将寄生虫从感染的红细胞中分离出来后，用2'5'-ADP-琼脂糖4B通过亲和色谱法纯化葡萄糖-6-磷酸脱氢酶。在醋酸纤维素电泳中，疟疾葡萄糖-6-磷酸脱氢酶与红细胞酶有显著差异。寄生虫特异性葡萄糖-6-磷酸脱氢酶的亚基分子量为55 kD，而红细胞酶的亚基分子量为59 kD。来自伯氏疟原虫的葡萄糖-6-磷酸脱氢酶与抗大鼠红细胞葡萄糖-6-磷酸脱氢酶的抗体无交叉反应。与宿主细胞酶相比，疟疾葡萄糖-6-磷酸脱氢酶对葡萄糖-6-磷酸的Km值增加了一个数量级。