Abstract
Summary
The characteristics of the bone acid phosphatase (EC 3.1.3.2) activity have been studied using both β-glycerophosphate and phenylphosphate as substrates. The acid β-glycerophosphatase activity was strongly inhibited by tartrate, fluoride, and molybdate and moderately inhibited by mercury. These properties are consistent with the presence of an enzyme similar to the major nonspecific acid phosphatase of the liver lysosomes.
The major characteristics of the acid phenylphosphatase activity were strong inhibition by fluoride and molybdate, but not by tartrate; strong activation by cysteine, dithio-threitol, and ascorbate and a moderate activation by malonate. The activation by cysteine was enhanced by the addition of Fe2+, Ni2+ or Cu2+. The properties and high activity demonstrated with the acid phenylphosphatase assay indicate the presence of a second enzyme in bone with properties similar to phosphoprotein phosphatase (EC 3.1.3.16).
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