Zn-dependent acid phosphatase from chicken’s heart was partially purified by ammonium sulfate precipitation, heat treatment at 60 °C, CM-Cellulose chromatography and gel filtration on Sephadex 0-100 to the specific activity of 08.pmol miri’ mg’ at pH 60. A 34efolds purification was achieved with the recovery of 8 %. The enzyme had molecular weight 57 kDa as revealed by gel filtration and 29 kDa by SDS polyacrylamide gel electrophoresis, indicating the dimeric nature of the enzyme. The enzyme was activated by ZrC, Co and Mn and inhibited by phosphate, hile EDTA, tartrate and flouride had little or no effect on the activity, which are the potent inhibitors of high molecular weight acid phospIatases.
A H SHAH ,A SAEED ,A R KHAN ,
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