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PMID: 5650366 Published · ppublish English Journal Article

Chromatography of oxidized and reduced cytochrome c on carboxymethylcellulose.

The Biochemical journal ·Vol. 107 ·No. 3 ·1968-04-00 ·Pages 427-31

Dixon HB, Thompson CM

Abstract

1. Cytochrome c was isolated from horse heart by a chromatographic method. 2. Oxidized and reduced cytochrome c were chromatographed on CM-cellulose that was in equilibrium with several buffer systems of constant composition at pH values of 8.4, 6.75 and 4.9. 3. Separation was better at the higher pH values; the oxidized form was retarded more than twice as much as the reduced form, though they differed by only a single charge. 4. Self-competition between cytochrome molecules is suggested to account for the peak distortion observed at high loads (above 20mum protein concentration).

MeSH Terms
Animals Buffers Chromatography, Ion Exchange Cytochromes/analysis Horses Hydrogen-Ion Concentration Methods Methylcellulose Myocardium/analysis Oxidation-Reduction
Chemicals
Buffers Cytochromes Methylcellulose
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Dixon H B
Thompson C M
References (5)
5 references, click to expand
  1. Cytochrome c.
    Adv Protein Chem. 1966;21:113-286 PMID: 5333288
  2. The chromatographic behaviour of cytochrome c on cation exchangers.
    Biochem J. 1954 Apr;56(4):535-43 PMID: 13159877
  3. Separation of neutral proteins on ion-exchange resins.
    Biochem J. 1955 Apr;59(4):543-52 PMID: 14363145
  4. A study of the cytochrome c haemochromogen.
    Biochem J. 1959 Mar;71(3):559-70 PMID: 13638265
  5. REMOVAL OF THE N-TERMINAL RESIDUE OF A PROTEIN AFTER TRANSAMINATION.
    Biochem J. 1965 Feb;94:463-9 PMID: 14346090
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1968-04-00
Pages
427-31
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1198680
Subset
IM
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