Primary structure of the large subunit of trifunctional beta-oxidation complex from pig heart mitochondria.
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.
Yang
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Department of Pharmacology, New York State Institute for Basic Research in Developmental Disabilities, Staten Island 10314.
He
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Styles
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Luo
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MJ
Schulz
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Elzinga
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D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry; D005227:Fatty Acids / Q000378:metabolism*; D008929:Mitochondria, Heart / Q000201:enzymology*; D063991:Mitochondrial Trifunctional Protein; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000737:chemistry*; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011498:Protein Precursors / Q000737:chemistry; D021382:Protein Sorting Signals / Q000737:chemistry; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid; D013552:Swine
D002352:Carrier Proteins; D005227:Fatty Acids; D009097:Multienzyme Complexes; D011498:Protein Precursors; D021382:Protein Sorting Signals; D063991:Mitochondrial Trifunctional Protein