title: The primary structure of aspartate aminotransferase from pig heart muscle. Partial sequences determined by digestion with thermolysin and elastase.
abstract: Peptides produced by thermolytic digestion of aminoethylated aspartate aminotransferase and of the oxidized enzyme were isolated and their amino acid sequences determined. Digestion by elastase of the carboxymethylated enzyme gave peptides representing approximately 40% of the primary structure. Fragments from these digests overlapped with previously reported sequences of peptides obtained by peptic and tryptic digestion (Doonan et al., 1972), giving ten composite peptides containing 395 amino acid residues. The amino acid composition of these composite peptides agrees well with that of the intact enzyme. Confirmatory results for some of the present data have been deposited as Supplementary Publication 50018 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973) 131, 5.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001219:Aspartate Aminotransferases / Q000032:analysis*; D002852:Chromatography, Ion Exchange; D008956:Models, Chemical; D009206:Myocardium / Q000201:enzymology*; D010196:Pancreatic Elastase; D010455:Peptides / Q000302:isolation & purification; D013552:Swine; D013820:Thermolysin
chemical_list: D010455:Peptides; D001219:Aspartate Aminotransferases; D010196:Pancreatic Elastase; D013820:Thermolysin