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Acylphosphatase was purified from horse muscle by a new procedure involving an affinity chromatography step and subsequent ion-exchange chromatography. This procedure was considerably milder than the preceding one, gave an overall yield of about 60% of activity and permitted isolation of three molecular forms with acylphosphatase activity. All these enzymatic forms are tightly bound to Sepharose 4B-linked anti-horse muscle acylphosphatase antibodies. Two of these forms (Ho1 and Ho3) are present in larger amounts: Ho1 corresponds to the enzyme purified according to the older procedure; this enzyme is a mixed disulfide between a main chain of 98 amino acid residues and glutathione. Ho2 differs from Ho1 only in the chemical nature of the molecule(s) S-S bound to the sole cysteine present at position 21 of the main chain. Ho3 is an S-S dimer of the main polypeptide chain. Ho1, Ho2, and Ho3 elicit very similar kinetic parameters in the presence of benzoylphosphate as a substrate.
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