Complete amino acid sequence of the ADP/ATP carrier from beef heart mitochondria

Abstract

The complete primary structure of the ADP/ATP carrier from beef heart mitochondria is described. Cyanogen bromide cleaves the protein into a long, N-terminally blocked fragment with Mr 22,000 (CB1) and several small peptides. The primary information was derived from liquid-phase sequencing of tryptic peptides obtained from the maleylated carrier protein and the citraconylated CB1 fragment, as well as from cleavage products with Staphylococcus aureus protease. The multitude of thermolysinolytic, tryptic, chymotryptic and peptic peptides was sequenced by manual methods. They rendered overlaps and further supported already known partial sequences. Also, the bridge between the published acidolytic C-terminal fragment A2 was thus obtained.