Primary structure of aspartate aminotransferase from horse heart and comparison with that of other homotopic and heterotopic isoenzymes.
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.
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
D007527:Isoenzymes; D009579:Nitrobenzoates; D010446:Peptide Fragments; D004228:Dithionitrobenzoic Acid; D001219:Aspartate Aminotransferases