The Amino-Acid Sequence of Porcine Adenylate Kinase from Skeletal Muscle.

1. Adenylate kinase (ATP: AMP phosphotransferase) has been purified 490-fold from porcine muscle with a final yield of 60 mg/kg muscle. 2. The amino-acid composition is Asp₁₁ Asn₂, Thr₁₄, Ser₁₁, Glu₁₉,, Gln₆, Pro₆, Gly_19>, Ala₆, Cyst₂, Val₁₇, Met₆, Ile₉, Leu₁₈, Tyr₇, Phe₅, Lys₂₁, His₂, Arrg₁₁. 3. The protein molecules a single polypeptide chain of 194 amino-acid residues with an acetylmethionine at the N-terminus and a lysine residue at the C-terminus. 4. Cyanogen bromide cleavage of carboxymethylated adenylate kinase yielded six fragments which were further degraded by using trypsin, chymotrypsin, thermolysin, subtilisin or α-protease. Sequence data on the resulting peptides are summarized in the present report, full details are given in a supplementary paper which has been deposited at CNRS from where copies can be obtained. 5. The primary structure of porcine adenylate kinase was given. [ABSTRACT FROM AUTHOR]