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. 1970 Jun;102(3):826–834. doi: 10.1128/jb.102.3.826-834.1970

Biochemical Properties of Trypanosomatid Lactate Dehydrogenases

C J Bacchi 1, E I Ciaccio 1, Kathleen M O'Connell 1, S H Hutner 1
PMCID: PMC247634  PMID: 5464273

Abstract

Lactate dehydrogenase (LDH, E.C.1.1.1.27) was found in supernatant (cytoplasmic enzyme) fractions of the trypanosomatid flagellates Trypanosoma conorhini and Crithidia fasciculata if 10 mm cysteine was present in the homogenizing medium. The T. conorhini LDH activity with pyruvate as substrate was increased 35% if 5 mm cysteine was also included in reaction mixtures. Km values for the T. conorhini enzyme were 3.3 × 10−4m with pyruvate, and 1.6 × 10−4m with α-ketobutyrate. Cysteine inhibited α-ketobutyrate reduction. Comparison of trypanosomatid and human serum LDH enzymes with respect to Km, substrate activity and inhibition, pH optima, and Ki values for oxalate and oxamate indicated that the trypanosomatid isoenzymes differed significantly from serum LDH. C. fasciculata LDH was extremely labile, since 59% of the activity was lost 90 min after isolation. The role of LDH enzymes in trypanosomatid metabolism is discussed, and the results are related to other trypanosomatid LDH enzymes. The comparison of homologous enzymes in host and parasite is discussed with regard to metabolic function and a possible model system for chemotherapy.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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