Multiple Forms of Acid Phosphatase in Cotyledons ofVigna mungoSeedlings

Abstract
Acid phosphatase from cotyledons of dark-grown Vigna mungo seedlings was separated into four forms (la, Ib, Ha and lib) by ion-exchanger column chromatographies. Each form of the acid phosphatase was characterized for its pH dependency, substrate specificity, thermal stability, activation energy, approximate molecular weight, and the effect of metal ions and other substances on its activity. Each form of the enzyme exhibited high activity towards ATP and ADP relative to their activity towards p-nitrophenylphosphate, but showed very low activity towards phytate, a major organic phosphate reserve in cotyledons. Among the four forms, lib was most distinguishable by its low molecular weight and the thermal enhancement of activity.

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