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Oxidation and reduction of cytochrome c by mitochondrial enzymes of Setaria cervi*

Published online by Cambridge University Press:  05 June 2009

N. Goyal  and
V.M.L. Srivastava
N. Goyal
Affiliation:
Division of Biochemistry, Central Drug Research Institute, Lucknow-226001, India
V.M.L. Srivastava*
Affiliation:
Division of Biochemistry, Central Drug Research Institute, Lucknow-226001, India
*
†Author for correspondence.
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Abstract

A mitochondria-rich fraction isolated from the cuticle-hypodermis-muscie system of Setaria cervi, a bovine filarial parasite, possessed substrate-coupled cytochrome c reductases and cytochrome c oxidase in appreciable activities. All these activities were located predominantly in the membranes. NADH-coupled cytochrome c reductase was more prominent than NADPH- and succinate-coupled reductases. All the three reductases exhibited marked sensitivity to rotenone and antimycin A. Salicylhydroxamic acid strongly inhibited succinate requiring reductase and cytochrome c oxidase, but the other two reductases only mildly. Sodium azide activated the reductases but substantially inhibited the oxidase activity. Potassium cyanide activated the succinate requiring reductase but did not cause any noticeable change in the activities of pyridine nucleotide linked reductases. Anthelmintics also influenced these activities but no definite correlation could be drawn regarding their mode of action.

Type
Research Papers
Information
Journal of Helminthology , Volume 69 , Issue 1 , March 1995 , pp. 13 - 17
Copyright
Copyright © Cambridge University Press 1995

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Footnotes

*

CDRI Communication No. 4960.

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