Glucose-6-phosphate dehydrogenase from Plasmodium berghei: kinetic and electrophoretic characterization.
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.
Institute of Biochemistry, School of Medicine (Charité), Humboldt-University, Berlin, G.D.R.
D
D
Buckwitz
G
G
Jacobasch
U
U
Kuckelkorn
D
D
Megow
D000818:Animals; D000906:Antibodies / Q000276:immunology; D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000276:immunology / Q000469:parasitology*; D005954:Glucosephosphate Dehydrogenase / Q000378:metabolism*; D007700:Kinetics; D010962:Plasmodium berghei / Q000201:enzymology* / Q000276:immunology; D051381:Rats
D000906:Antibodies; D005954:Glucosephosphate Dehydrogenase