Purification and characterization of rabbit muscle acylphosphatase in the thiol (‐SH) form

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Abstract
Modifications in the muscle acylphosphatase purification procedure enabled us to isolate the enzyme with its sole cysteine in the ‐SH form; this enzyme form is the most abundant in vivo. Our data demonstrate that the enzyme forms purified by previously reported procedures can be easily derived from a reaction of the SH‐enzyme with oxidized glutathione. Probably most, or even all, of these enzyme forms are artifacts due to the purification. The SH‐acylphosphatase shows kinetic parameters similar to those reported for the mixed disulfide with glutathione and S‐S dimer, except for the specific activity value, which is about twice as much, and the Km, which is reduced.