Berti A, Tremori E, Pazzagli L, Degl'Innocenti D, Camici G, Cappugi G, Manao G, Ramponi G
Department of Biochemical Sciences, University of Florence, Italy.
J Protein Chem. 1991 Feb;10(1):91-102. doi: 10.1007/BF01024659.
Acylphosphatase was purified from rat skeletal muscle essentially by gel filtration and high-performance ion-exchange chromatography. The complete amino acid sequence was reconstructed by using the sequence data obtained from tryptic, peptic, and S. aureus V8 protease peptides. The protein consists of 96 amino acid residues and is acetylated at the NH2-terminus. The immunological cross-reactivity of acylphosphatase from rat and horse skeletal muscle was examined by ELISA. The reaction with rabbit antiserum revealed the presence of at least five antigenic sites on rat enzyme, two of which are common to horse muscle enzyme. Anti-rat antibodies also recognize the peptide that corresponds to the initial part of the molecule, which varies greatly from equine enzyme. Two completely new antigenic sites are herein described: the first can be considered the main antigenic site and is located within positions 21-36, the second is in the COOH-terminal part of the molecule. A mixture of immunoreactive peptides gives strong antibody-antigen reaction inhibition (94%).
