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    Biochem Mol Biol Int. 1993 Jun;30(2):253-60.

    Isolation and characterization of the ND2 polypeptide of the bovine energy-transducing NADH-ubiquinone oxidoreductase (complex I).

    Yagi T.

    Department of Molecular and Experimental Medicine, Scripps Research Institute, La Jolla, California 92037.

    The M(r) 30,000 polypeptide of the hydrophobic protein fraction of the energy-transducing NADH-ubiquinone oxidoreductase (complex I) of bovine heart mitochondria was identified as the ND2 gene product based on a comparison of amino acid analysis and partial N-terminal sequencing results with the known DNA sequence of ND2 (Anderson, S. et al. (1982) J. Mol. Biol. 156, 683-717). A simple purification procedure was devised for this ND2 gene product. The procedure, which is described, involves treatment of bovine complex I with a chloroform-methanol (2:1 [v/v]) solution. The antiserum raised against this purified bovine ND2 gene product cross-reacted with the approximately M(r) 39,000 polypeptide extracted from the Paracoccus denitrificans membranes with chloroform-methanol (2:1 [v/v]).

    PMID: 8364407 [PubMed - indexed for MEDLINE]

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