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    Biochem Biophys Res Commun. 1994 Jan 28;198(2):431-7.

    Primary structure of the large subunit of trifunctional beta-oxidation complex from pig heart mitochondria.

    Yang SY, He XY, Styles J, Luo MJ, Schulz H, Elzinga M.

    Department of Pharmacology, New York State Institute for Basic Research in Developmental Disabilities, Staten Island 10314.

    The amino-terminal and internal sequences of the isolated large subunit of trifunctional beta-oxidation complex from pig heart mitochondria were determined by Edman degradation. The results demonstrated that the sequence of this novel beta-oxidation enzyme is identical with the sequence recently reported for a porcine gastrin binding protein that serves as the gastrin receptor on parietal cell surfaces. Evidence is provided to show that it is unlikely that the porcine gastrin binding protein has such a sequence. The data lead us to conclude that the mature large subunit of porcine trifunctional beta-oxidation complex is composed of 727 amino acid residues with a calculated molecular weight of 79,113, while the precursor of this long-chain fatty acid oxidation enzyme has a mitochondrial presequence consisting of 36 residues and a calculated M(r) of 83,099.

    PMID: 8297352 [PubMed - indexed for MEDLINE]

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