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Purification of cytochrome oxidase by using sepharose-bound cytochromec

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
65
Issue
3
Identifiers
DOI: 10.1016/s0006-291x(75)80499-2
Disciplines
  • Biology

Abstract

Summary Cytochrome oxidase, a typical membrane enzyme, was purified by a simple procedure using immobilized cytochrome c. Sepharose-bound cytochrome c packed in a column was reduced with ascorbate. A cytochrome oxidase sample prepared from mitochondrial inner membrane was charged onto the column. Proteins containing no heme a were eluted from the column in the void volume. The oxidase was then eluted with increasing concentration of deoxycholate. The purified oxidase contains 13.6 nmoles heme a per mg protein, i.e. has a minimum mass of 73,500 daltons per heme a.

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