| Abstract: | Acid phosphatase from cotyledons of dark-grown Vigna mungo seedlingswas separated into four forms (la, Ib, Ha and lib) by ion-exchangercolumn chromatographies. Each form of the acid phosphatase wascharacterized for its pH dependency, substrate specificity,thermal stability, activation energy, approximate molecularweight, and the effect of metal ions and other substances onits activity. Each form of the enzyme exhibited high activitytowards ATP and ADP relative to their activity towards p-nitrophenylphosphate,but showed very low activity towards phytate, a major organicphosphate reserve in cotyledons. Among the four forms, lib wasmost distinguishable by its low molecular weight and the thermalenhancement of activity. |
