Complete amino acid sequence of porcine heart citrate synthase

Publisher Website
Google Scholar
Abstract
The detailed proof of the 437-residue amino acid sequence (MW 48,969) of porcine heart citrate synthase is described. The S-carboxymethylated protein was cleaved at methionine (cyanogen bromide) and arginine (trypsin digest of citraconylated enzyme) residues to yield 14 and 17 major peptides, respectively. Peptides were initially fractionated by gel filtration, and those useful for sequence analysis were purified by high-performance liquid chromatography. Sequence analyses were performed on these primary peptides and on subpeptides generated by cleavage with the Br adduct of 2-[(2-nitrophenyl)sulfenyl]-3-methylindole, Staphylococcus aureus V8 protease, trypsin, chymotrypsin, or acid. The overall sequence was confirmed by analyzing products of cleavage by hydroxylamine, acid and subtilisin. A novel feature of the sequence is the identification of trimethyllysine at residue 368.