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Enzymes of Carbohydrate Metabolism in Leishmania donovani Amastigotes 1
Author(s) -
MEADE JOHN C.,
GLASER THERESA A.,
BONVENTRE PETER F.,
MUKKADA ANTONY J.
Publication year - 1984
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1984.tb04307.x
Subject(s) - biochemistry , citric acid cycle , biology , pentose phosphate pathway , amastigote , enzyme , metabolism , pyruvate carboxylase , leishmania , glycolysis , parasite hosting , world wide web , computer science
A method for the isolation of Leishmania donovani amastigotes from infected hamster spleen and liver tissues is described. Over 85% of the isolated amastigotes were viable as judged by acridine orange‐ethidium bromide staining and in vitro transformation to the promastigote form. A comprehensive survey of the enzymes of carbohydrate metabolism in L. donovani amastigotes and promastigotes was conducted. Amastigotes and promastigotes possess all of the enzymes of the Embden‐Meyerhof pathway, hexose monophosphate shunt, and tricarboxylic acid cycle. Cell‐free extracts of both forms show pyruvate dehydrogenase activity which permits entry of pyruvate into the tricarboxylic acid cycle. Both forms demonstrate an active glutamate dehydrogenase, thus linking amino acid metabolism with carbohydrate metabolism. Pyruvate carboxylase, the enzyme responsible for replenishment of C 4 acids by heterotrophic CO 2 fixation into pyruvate, was also demonstrable in the tissue and insect forms. In general, activities of promastigote enzymes are higher than the amastigote enzymes. Differences between the vertebrate (amastigote) and invertebrate (promastigote) forms in their potential to utilize carbohydrates as substrates would appear to be quantitative rather than qualitative.