Camici G, Manao G, Stefani M, Berti A, Cappugi G, Liguri G, Ramponi G
Ital J Biochem. 1984 Jan-Feb;33(1):1-16.
Turkey muscle acylphosphatase is strongly bound to anti-(horse muscle acylphosphatase ) antibodies covalently linked to an agarose resin. This permits use of an affinity chromatography step in the purification, which increased the final yield and allowed us to isolate three different molecular forms of the enzyme. Form 1 is a mixed disulfide between the polypeptide chain and glutathione; form 3 is an S-S dimer of the polypeptide chain present in form 1, while form 2, present in a very low amount, consists of a polypeptide chain quite similar in aminoacid composition to that found in form 1. The three molecular forms show very similar kinetic parameters. The comparison of these molecular forms with those isolated from horse muscle showed similar kinetic properties but different structural features.
