Abstract
Alkaline inorganic pyrophosphatase from corn leaves has been purified 1750-fold by fractionation with (NH 4) 2SO 4 and Ca 3(PO 4) 2 gel followed by DEAE-cellulose column chromatography. The enzyme which chromatographed as a single peak on DEAE-cellulose, required Mg 2+ for activity at a pH optimum of 8·3–8·8. The preparation was devoid of Mg 2+ inhibited acid pyrophosphatase. The enzyme exhibited a high specificity for inorganic pyrophosphate as substrate to the virtual exclusion of several phosphorylated organic compounds. Both mono- and di-magnesium pyrophosphate were substrates for the enzyme, the greater activity occurring with the mono-magnesium salt. The enzyme was inhibited by fluoride and several divalent cations excepting Cu.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
