Structures of Beef Mitochondrial Complex I Subunits

  • Sadao Wakabayashi
  • Ryoji Masui
  • Hiroshi Matsubara
  • Youssef Hatefi

Summary

Nine polypeptides were isolated from the iron-protein fragment of beef heart mitochondrial complex I. Their apparent molecular weights were estimated to be 75K, 49K, 30K, 20K, 18K, 15K, and 13K by SDS-polyacrylamide gel electrophoresis. Among them both the 30K and 13K bands each contained two distinct polypeptides. The amino acid analysis of each subunit suggested that the 75K, 49K, two 30K, 20K, 15K and one of the 13K polypeptides had enough cysteines and histidines to chelate the iron-sulfur clusters. The amino acid sequences of the 13K polypeptides were determined to show no apparent structural similarity to other proteins.

Keywords

HPLC Urea Cysteine Polypeptide Glutamine 

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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Sadao Wakabayashi
    • 1
  • Ryoji Masui
    • 1
  • Hiroshi Matsubara
    • 1
  • Youssef Hatefi
    • 2
  1. 1.Department of BiologyOsaka UniversityToyonaka, Osaka 560Japan
  2. 2.Division of BiochemistryScripps Clinic and Research FoundationLa JollaUSA

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