Detection of a system of microsomal monooxygenases in a malaria parasite of rodents, Plasmodium berghei

Microsomes were isolated from cells of the malaria parasite of Plasmodium berghei . The spectral characteristics of the microsome preparations indicate the presence of cytochromes b sub(5)and P-420 in P. berghei) microsomes. In the electrophoretic separation of microsome proteins of P. berghei , pro...

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Published inBiochemistry (Easton) Vol. 52; no. 3; pp. 327 - 331
Main Authors Chekhonadskikh, T V, Polyakova, N E, Pankova, T G, Salganik, R I
Format Journal Article
LanguageEnglish
Published 01.01.1987
Subjects
Plasmodium berghei
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Summary:Microsomes were isolated from cells of the malaria parasite of Plasmodium berghei . The spectral characteristics of the microsome preparations indicate the presence of cytochromes b sub(5)and P-420 in P. berghei) microsomes. In the electrophoretic separation of microsome proteins of P. berghei , proteins were detected, corresponding in molecular weight to NADPH-cytochrome c reductase, cytochrome P-450, and epoxide hydratase. The activity of NADPH-cytochrome c reductase and benzpyrene hydroxylase was determined. The spectral characteristics, results of electrophoresis of microsomal proteins, and enzymatic activities indicate the presence of a P-450-containing system of monooxygenases in the plasmodium. The relationship of the activity of this system to the resistance of the plasmodium to the antimalarial drug chloroquine is discussed.
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ISSN:0006-2960