Abstract
Summary Acid phosphatase (EC 3.1.3.2) of C. reflexa appears to be a soluble enzyme. Cell-disruption in a medium containing cysteine, NaCl and EDTA resulted in a maximally active preparation. Immediate sequential heat treatment and passage through Sephadex G-25 of the 16,000 · g extract stabilised the enzyme preparation. The subsequent ammonium sulfate fractionation between 50–100% saturation followed by passage through Sephadex G-75 and thenDEAE-cellulose column resulted in about 300-fold enrichment of the enzyme with 10—15% recovery. The enzyme exhibits a pH optimum of 3.5, km of 5 × 10− 6 M against BGP1 is a fairly heat stable enzyme, unspecific in nature, with minimal (about 25%) action towards GIP and FDP, is slightly (about 15%) inhibited by Mg2+ and Mn2+, completely inhibited by Cu2+ and Zn2+ and molybdate and fluoride act as non-competitive and competitive inhibitors respectively, with a ki for Mo2+ of 1.5 × 10− 8M and that for F− of 1.9 × 10− 9 M.
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