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PURIFICATION AND PROPERTIES OF LACTATE DEHYDROGENASE FROM PLASMODIUM KNOWLESI AND ERYTHROCYTES OF THE RHESUS MONKEY
Author(s) -
Saxelini,
Pandey VC,
Dutta GP,
Ghatak S
Publication year - 1986
Publication title -
australian journal of experimental biology and medical science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0004-945X
DOI - 10.1038/icb.1986.6
Subject(s) - plasmodium knowlesi , thermostability , lactate dehydrogenase , enzyme , parasite hosting , biology , polyacrylamide gel electrophoresis , biochemistry , affinity chromatography , microbiology and biotechnology , molecular mass , malaria , plasmodium falciparum , plasmodium vivax , immunology , world wide web , computer science
Summary Lactate dehydrogenase, E.C.1.1.1.27 (LDH) from the simian malarial parasite, Plasmodium knowlesi , and from normal rhesus monkey erythrocytes has been purified using Blue Sepharose affinity chromatography, and the properties of the purified enzyme from these two sources have been compared. The enzyme from the host and parasite were different in their kinetic properties, viz., substrate and pH optima, thermostability and isoenzymic behaviour. Partially purified LDH of the erythrocytes resolved into three isomeric bands on polyacrylamide gel electrophoresis, whereas the parasite LDH moved as a single enzyme band of different mobility from the host LDH. The molecular mass of the parasite enzyme was estimated as 117,500 daltons.