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On Glycolysis in Trichomonas vaginalis
Author(s) -
WELLERSON RALPH,
KUPFERBERG ALFRED B.
Publication year - 1962
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.1550-7408.1962.tb02646.x
Subject(s) - glycolysis , trichomonas vaginalis , glycogen phosphorylase , biochemistry , enzyme , biology , glycogen , citric acid cycle , chemistry , microbiology and biotechnology
SYNOPSIS. The mechanism of carbohydrate dissimilation was studied in cell‐free extracts prepared from mass cultures of the trichomonads. Evidence for the presence of all the enzymes associated with the Embden‐Meyerhof glycolytic scheme was obtained. Several enzyme systems directly associated with the glycolytic pathway were examined. Two of these, alcohol dehydrogenase and phosphorylase, were not demonstrated in the T. vaginalis extract. The absence of phosphorylase in the presence of a very high glycogen concentration in the cell (20.8%) suggests the possibility of an alternate route. A very active TPN‐linked “malic enzyme” was also demonstrated, although no functional citric acid cycle is known for this trichomonad. Based on the experimental evidence and collateral data, a functional Embden‐Meyerhof system was suggested for T. vaginalis.