COMPLETE AMINO-ACID-SEQUENCE OF THE ADP ATP CARRIER FROM BEEF-HEART MITOCHONDRIA

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  • 1 January 1982
    • journal article
    • research article
    • Vol. 363  (3) , 345-349
Abstract
The complete primary structure of the ADP/ATP carrier from beef heart mitochondria is described. CNBr cleaves the protein into a long, N-terminally blocked fragment with MW 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 many thermolysinolytic, tryptic, chymotryptic and peptide peptides were 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 obtained.

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