The primary structure of mitochondrial aspartate aminotransferase from pig heart: peptides obtained by cleavage at basic residues.

S Doonan, H M Fahmy, G J Hughes, D Barra, F Bossa

Index: Ital. J. Biochem. 28(6) , 441-55, (1979)

Full Text: HTML

Abstract

Results obtained as part of a study of the primary structure of mitochondrial aspartate aminotransferase from pig heart are described. In particular, the S-aminoethylated protein was digested with trypsin and with the lysine specific protease from A. mellea. In the first case peptides contained 221 out of the total of 401 amino acid residues in the protein were obtained. By contrast the digest with A. mellea protease was not examined exhaustively and six peptides containing 49 amino acid residues were isolated. Digestion of the trifluoroacetylated and S-aminoethylated protein with A. mellea protease yielded a mixture of large fragments three of which, containing 89 amino acid residues, are described here. The combined results of these three digests yielded 66.6% of the total structure, concentrated mainly in the N-terminal half of the protein.