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Steady‐State Oxvgen Kinetics of Terminal Oxidases in Trypanosoma mega *
Author(s) -
HILL GEORGE C.,
DEGN HANS
Publication year - 1977
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.1550-7408.1977.tb01015.x
Subject(s) - alternative oxidase , salicylhydroxamic acid , cytochrome c oxidase , sodium azide , oxidase test , azide , kinetics , biochemistry , chemistry , mega , enzyme , physics , organic chemistry , quantum mechanics , astronomy
SYNOPSIS. Steady‐state oxygen kinetics of Trypanosoma mega reveal the presence of 3 oxidases. These include an oxidase which is sensitive to salicylhydroxamic acid (SHAM) but insensitive to sodium azide. This oxidase could be the L‐α glycerophosphate oxidase present in bloodstream trypanosomes. In addition, an oxidase is present which is azide‐sensitive but SHAM‐insensitive. This oxidase is inhibited by CO and is probably cytochrome aa 3 . A 3rd oxidase is insensitive to both azide and SHAM but is inhibited by CO and is possibly cytochrome o. Reciprocal plots of T. mega reveal the presence of 2 oxidases that are inhibited by CO. These results are discussed in the light of previous evidence suggesting the presence of several oxidases and a branched electron transport system in T. mega .