PURIFICATION AND PROPERTIES OF LACTATE DEHYDROGENASE FROMPLASMODIUM KNOWLESIAND ERYTHROCYTES OF THE RHESUS MONKEY
作者:
Nalini Saxena,
VC Pandey,
GP Dutta,
S Ghatak,
期刊:
Australian Journal of Experimental Biology and Medical Science
(WILEY Available online 1986)
卷期:
Volume 64,
issue 1
页码: 53-61
ISSN:0004-945X
年代: 1986
DOI:10.1038/icb.1986.6
出版商: Nature Publishing Group
数据来源: WILEY
摘要:
SummaryLactate 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.
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