Multiple Forms of Acid Phosphatase in Cotyledons ofVigna mungoSeedlings

Isolation and enzymatic properties of a nonspecific acid phosphatase from Vigna aconitifolia seeds

“…In our experiment, we observed only one isoform of AP from V. aconitifolia during chromatography and could not trace the activity for AP while washing the column with Na‐acetate buffer containing 0.5 N NaCl and 1 N NaCl, which neglects the possibility of the presence of AP bound to the CM‐cellulose column. However, Ninomiya et al and Tamura et al have observed the activity for AP both in the unbound as well as in the bound fraction of the cation exchange column . Specific activity of AP purified in our experiment (29.6 U mg −1 protein) was higher in comparison with AP purified by Tamura et al , Miernyk , and Cabello‐Diaz et al from Vigna mungo cotyledons (Peak Ib: 3 U mg −1 , peak IIa: 1.5 U mg −1 protein), maize endosperm culture (2.6 U mg −1 protein), and Phaseolus vulgaris (18.1 U mg −1 protein), respectively.…”

“…However, Ninomiya et al and Tamura et al have observed the activity for AP both in the unbound as well as in the bound fraction of the cation exchange column . Specific activity of AP purified in our experiment (29.6 U mg −1 protein) was higher in comparison with AP purified by Tamura et al , Miernyk , and Cabello‐Diaz et al from Vigna mungo cotyledons (Peak Ib: 3 U mg −1 , peak IIa: 1.5 U mg −1 protein), maize endosperm culture (2.6 U mg −1 protein), and Phaseolus vulgaris (18.1 U mg −1 protein), respectively. However, it was much lower than the specific activity reported for AP from various other plant sources such as banana fruit (745 U mg −1 protein), Euphorbia latex (598 U mg −1 protein), and tobacco cell wall (494 U mg −1 protein) .…”

“…Cu 2+ , Fe 3+ , molybdate, fluoride, and phosphate ions acted as strong inhibitors for the enzyme purified in our experiment. These ions are reported as inhibitors also for AP isolated from other various sources . In addition, Zn 2+ , Mn 2+ , and Fe 2+ inhibited the enzyme activity by more than 70% at higher concentrations (5 mM).…”

“…The present study deals with the purification of AP from Vigna aconitifolia seeds and explores its physicochemical properties. Currently, there are few reports on AP from other Vigna plant sources that describe biochemical properties of its various isozymes . So, this study could contribute valuable information about this ubiquitous enzyme.…”

A Review Bioactive Components of Vigna mungo

“…It was separated into four forms which are different from each other in their properties such as substrate specificity, thermal stability, molecular weight and susceptibility to metal ions and other substances. [22] Acid phosphatase was isolated by using a combination of column chromatography and gel electrophoresis from cotyledons of Vigna mungo seedlings is composed of at least six forms (la, Ia2, Ib, Ib2, Ha and lib). They examined the immunological relationships between the multiple forms from cotyledons and the distribution of the enzyme in organs of maturing and germinating seed.…”