Abstract
Riboflavin kinase and FAD-pyrophosphorylase have successfully separated from bovine fetus heart by using DEAE-Sephadex column chromatography under a gradient elution with Tris-HCl buffer. Specific activity of each enzymes raised up to 20 (FAD-pyrophorylase) or to 82 fold (riboflavin kinase) comparing with those of the original extracts. The purified riboflavin kinase showed the optimal pH at 7.5,with the Michaelis constant of 5.03×10^<-5>M, and the activation energy was 13,180 cal/mole at 5 to 15℃, while in FAD-pyrophosphorylase, the optimal pH, Michaelis constant, and the activation energy were 8.2,2.56×10^<-4>M, and 4,521 cal/mole, respectively.
