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Evidence of Lactate Dehydrogenase in Anaplasma marginale

Department of Veterinary Science, Agricultural Experiment Station, Louisiana State University, Baton Rouge, Louisiana
Department of Microbiology, Louisiana State University, Baton Rouge, Louisiana

ABSTRACT

Extracts from preparations of partially purified Anaplasma marginale revealed low levels of lactate dehydrogenase (LDH). Enzyme inhibition by immune sera further indicated that A. marginale possesses a protein moiety the same as that of the normal red blood cell (RBC), although data suggested an alteration of LDH₁ from that observed in normal RBC. Bimodal isozyme distribution was detected after electrophoresis of the extracts. One isozyme approached the cathode and the other the anode, and both appeared to be nicotinamide adenine dinucleotide-dependent. Heterogeneity of parasite and host cell isozymes was established on the basis of zone electrophoresis on cellulose acetate strips.

¹ Present address: The University of Texas, M. D. Anderson Hospital and Tumor Institute, Department of Biochemistry, Houston.

² Present address: Department of Microbiology, Northwestern State College of Louisiana, Natchitoches.