Identification and Partial Purification of a Stage-Specific 33 kDa Mitochondrial Protein as the Alternative Oxidase of the Trypanosoma brucei brucei Bloodstream Trypomastigotes

1995 ◽  
Vol 42 (5) ◽  
pp. 467-472 ◽  
Author(s):  
MINU CHAUDHURI ◽  
WILFRED AJAYI ◽  
STARLETT TEMPLE ◽  
GEORGE C. HILL
1992 ◽  
Vol 70 (2) ◽  
pp. 136-141 ◽  
Author(s):  
Jack A. Kornblatt ◽  
Joseph Nthale ◽  
Francis McOdimba

A protein has been purified from the membranes of bloodstream forms of Trypanosoma brucei brucei. The purified material contained a single polypeptide chain of molecular mass 67 kilodaltons as judged by sodium dodecyl sulfate –polyacrylamide gel electrophoresis; under "native" conditions it migrated through a Sephacryl S-300 column with a similar molecular mass. The purified protein catalysed electron transfer from sn-glycerol 3-phosphate to oxygen with the subsequent formation of water. Electron transfer by the purified enzyme to O2 was dependent on the presence of low concentrations of the mediator phenazine methosulfate. This protein is clearly the major membrane-bound sn-glycerol-3-phosphate dehydrogenase, but it also has some characteristics suggestive of the trypanosome alternative oxidase activities.Key words: trypanosomes, glycerophosphate dehydrogenase, trypanosome alternative oxidase.


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Author(s):  
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Sedrick Anderson ◽  
Alex Chipeleme ◽  
Minu Chaudhuri ◽  
...  

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