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The amino acid sequences of 39 tryptic peptides from carboxymethylated mitochondrial aspartate aminotransferase from pig heart muscle were analyzed. The peptides were purified by gel filtration, ion exchange column chromatography, paper chromatography, and high voltage paper electrophoresis, and their sequences were examined by manual Edman degradation, carboxypeptidase digestion, and fragmentation with thermolysin or chymotrypsin. These peptides accounted for 318 of the total 401 amino acid residues in the protein subunit.
Kagamiyama et al. (Fri,) studied this question.
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