Purification of sn-glycerol-3-phosphate dehydrogenase from Trypanosoma brucei brucei.
Biochem Cell Biol
; 70(2): 136-41, 1992 Feb.
Article
en En
| MEDLINE
| ID: mdl-1510824
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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Trypanosoma brucei brucei
/
Glicerolfosfato Deshidrogenasa
Límite:
Animals
Idioma:
En
Revista:
Biochem Cell Biol
Asunto de la revista:
BIOQUIMICA
Año:
1992
Tipo del documento:
Article
País de afiliación:
Canadá
Pais de publicación:
Canadá