Alkaline P - Glycerophosphatase of Green Gram * (

During the course of investigations on riboflavin 5’-phosphate and flavin adenine dinucleotide-hydrolyzing enzymes in green gram (Phaseolus radiatus), we observed that crude extracts possessed high phosphatase activity against a variety of phosphorylated compounds. Despite intensive studies on the animal phosphatases, plant phosphatases have received very little attention. Pfankuch (1) purified phosphatase from potato and sugar beet by alcohol precipitation. Later Giri (2) obtained highly active preparations of phosphatase from soya bean (Glycine hispida). A nonspecific phosphomonoesterase has been reported in green gram by Giri (3) ; later Ramanarayanan and Giri (unpublished observations) made a detailed study of the effect of molybdenum on the acid /3-glycerophosphatase and inorganic pyrophosphatase of green gram. Previous attempts by several workers to demonstrate the presence of an alkaline glycerophosphatase in plants have not been successful. Naganna et al. (4, 5) have reported a magnesium-activated alkaline pyrophosphatase in potato. Racker and Schroeder (6) demonstrated the occurrence of a specific fructose diphosphatase with maximal activity at pH 8.5. This paper describes a method of partial purification of an alkaline P-glycerophosphatase of green gram which is activated by ferric ion, and also some of its general properties.