Partial Purification and Characterisation of Acid Phosphatases from Developing Chickpea Seeds

Activity of acid phosphatases in chickpea seeds was found to be highest at the early stage of pod development (14 days after flowering). Acid phosphatases were therefore purified from seeds at early stage by DEAE-cellulose column chromatography followed by gel permeation chromatography, as three partially purified forms which were designated as acid phosphatase-1, acid phosphatase-2 and acid phosphatase-3. These forms were separately studied for their kinetic properties. All three forms had optimum pH of 5.5, optimum temperature of 55–60^oC but differed in substrate specificity. Pyrophosphate and p-nitrophenylphosphate were good substrates, phytic acid poor substrate and 3-phosphoglycerate and adenosine-tri-phosphate differed for their preference for all three forms of enzyme. Activities of these forms respond differently to various metal ions and chelating agents.