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Home / Equine Research Bank / Biochem J / The action of cyanogen bromide on horse-heart cytochrome c a...
The Biochemical journal1965; 96(3); 693-699; doi: 10.1042/bj0960693

The action of cyanogen bromide on horse-heart cytochrome c and horse-heart myoglobin.

Abstract: 1. The effects of cyanogen bromide on horse-heart cytochrome c and horse-heart myoglobin have been investigated. Cytochrome c yielded four fragments, of which two were haemopeptides. The two colourless peptides had amino acid compositions corresponding to those that are expected, on the basis of the sequence proposed for horse-heart cytochrome c by Margoliash, Smith, Kreil & Tuppy (1961), from cleavage at both methionine residues. Of the two haemopeptides, one was isolated and shown to be that derived from cleavage at only one methionine residue, that nearer to the C-terminus of the peptide chain. 2. Myoglobin also gave four peptides, three of which accounted for the total amino acid content of the intact protein. The fourth fragment arose by cleavage at a single methionine residue, that nearer the C-terminus. Characterization of this fourth fragment made it possible to deduce the order of arrangement of the fragments in the intact molecule.
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Publication Date: 1965-09-01 PubMed ID: 5862409PubMed Central: PMC1207205DOI: 10.1042/bj0960693Google Scholar: Lookup
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  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research explored the effects of cyanogen bromide on horse-heart cytochrome c and horse-heart myoglobin, yielding multiple fragments from both. An analysis of these fragments allowed the study to deduce the arrangement of components in the intact proteins.

Study Methodology and Findings

  • The research used cyanogen bromide as an experimental agent to investigate its effects on two types of proteins found in horse heart, namely cytochrome c and myoglobin.
  • Through this process, four fragments were derived from cytochrome c. Two of these fragments contained a haem group, commonly known as haemopeptides. The remaining two were colourless peptides. By analyzing the amino acid compositions of these colourless peptides, they matched expected values based on previously proposed sequences for horse heart cytochrome c.
  • The exact source of the two haemopeptides was identified. One was specifically derived from cleaving at one methionine residue. This residue was closer to the C-terminus of the peptide chain, the end to which new amino acids are added during protein biosynthesis.

Analysis of Myoglobin

  • Myoglobin also yielded four peptides following the application of cyanogen bromide. Three of these were accountable for the total amino acid content of the intact protein.
  • The fourth peptide was a product of cleavage at a single methionine residue. Similar to the cytochrome c analysis, this methionine residue was located nearer to the C-terminus of the peptide.
  • Through characterization of this fourth fragment, it was possible to deduce the order of arrangement of the fragments in the intact myoglobin molecule. This provides valuable insight into the molecular structure of myoglobin, which serves specific functions in muscle tissue, particularly in its storage and diffusion of oxygen.

In conclusion, this study provides valuable knowledge on the impact of cyanogen bromide on horse-heart cytochrome c and horse-heart myoglobin. Results from this study provide a better understanding of the structure of cytochrome c and myoglobin, and this can lead to a deeper comprehension of their role and behavior in biological systems.

Cite This Article

APA
Black JA, Leaf G. (1965). The action of cyanogen bromide on horse-heart cytochrome c and horse-heart myoglobin. Biochem J, 96(3), 693-699. https://doi.org/10.1042/bj0960693

Publication

The Biochemical journal
ISSN: 0264-6021
NlmUniqueID: 2984726R
Country: England
Language: English
Volume: 96
Issue: 3
Pages: 693-699

Researcher Affiliations

Black, J A
    Leaf, G

      MeSH Terms

      • Amino Acids
      • Animals
      • Bromides
      • Chemical Phenomena
      • Chemistry
      • Chromatography, Gel
      • Chromatography, Paper
      • Cyanides
      • Cytochromes
      • Horses
      • In Vitro Techniques
      • Myocardium
      • Myoglobin
      • Peptides

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      This article includes 18 references
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      Citations

      This article has been cited 1 times.
      1. Wallace CJ, Offord RE. The semisynthesis of fragments corresponding to residues 66-104 of horse heart cytochrome c. Biochem J 1979 Apr 1;179(1):169-82.
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