The primary structure of mitochondrial aspartate aminotransferase from pig heart: peptides obtained by cleavage with thermolysin and chymotrypsin

Abstract

The production, purification and analysis of peptide derived by digestion of mitochondrial aspartate aminotransferase with thermolysin and chymotrypsin are described. Despite the complexity of the peptide mixture obtained and the relative shortness of the fragments produced, these digests proved to be very useful for the completion of the primary structure determination of the enzyme. In fact, information for 87% of the total structure was contributed by thermolytic peptides, and for 89% by the chymotryptic ones. Moreover some of these peptides were essential for elucidating controversial points of the sequence.