title: Primary structure of aspartate aminotransferase from horse heart and comparison with that of other homotopic and heterotopic isoenzymes.
abstract: Sulphydryl groups of mitochondrial aspartate aminotransferase from horse heart were titrated with 5,5'-dithiobis (2-nitrobenzoic acid). From analysis of peptic peptides, 378 amino acid residues (94.3% of the total) in the protein were identified. The results of amino acid sequence analysis are compared with those of cytosolic and mitochondrial aspartate aminotransferases from other sources.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001219:Aspartate Aminotransferases / Q000378:metabolism*; D004228:Dithionitrobenzoic Acid / Q000494:pharmacology*; D006736:Horses; D007527:Isoenzymes / Q000378:metabolism; D008929:Mitochondria, Heart / Q000201:enzymology*; D009579:Nitrobenzoates / Q000494:pharmacology*; D010446:Peptide Fragments / Q000032:analysis; D013045:Species Specificity
chemical_list: D007527:Isoenzymes; D009579:Nitrobenzoates; D010446:Peptide Fragments; D004228:Dithionitrobenzoic Acid; D001219:Aspartate Aminotransferases