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The complete amino acid sequence of horse muscle acylphosphatase.
The amino acid sequence of horse muscle acylphosphatase is given in the present paper. The carboxymethylated enzyme consists of a single polypeptide chain of 98 amino acid residues with an acetyl group blocking the NH2 terminus and a tyrosine at the COOH terminus. The calculated molecular weight of the native protein, a mixed disulfide with glutathione, is 11,365. The carboxymethylated protein was cleaved by cyanogen bromide. The three expected fragments were purified; moreover, an additional fragment, derived from a partial failure of cleavage at methionine-24, was purified and characterized. The structures of the cyanogen bromide fragments were established by subfragmentation with endopeptidases, and the sequences of the overlapping subfragments were determined. From the results, it was possible to order the peptides within the sequence and then to establish the complete primary structure of the enzyme.
PMID: 6248536 [PubMed - indexed for MEDLINE]
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Cited by 2 PubMed Central articles
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Mechanism of acylphosphatase inactivation by Woodward's reagent K.
Paoli P, Fiaschi T, Cirri P, Camici G, Manao G, Cappugi G, Raugei G, Moneti G, Ramponi G.
Biochem J. 1997 Dec 15; 328 ( Pt 3):855-61.
[Biochem J. 1997]
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Studies on synthesis and degradation rates and some molecular properties of guinea-pig muscle acylphosphatase.
Liguri G, Nassi P, Camici G, Manao G, Cappugi G, Stefani M, Berti A, Ramponi G.
Biochem J. 1984 Jan 15; 217(2):499-505.
[Biochem J. 1984]