Abstract
Riboflavin kinase and FAD-pyrophosphorylase have been partially purfied and separated from pig liver, by means of ammonium sulfate fractionation and the distributions of both enzymes in various organs and cell fractions were also demonstrated. Riboflavin kinase was particularly rich in mucous membrane of mouse small intestine, in contrast, FAD-pyrophosphorylase was abundantly distributed in spleen, liver, and heart. Among mammalian livers, the activity of FAD-pyrophosphorylase was the highest in human fetus liver, however, about one-sixth in normal adult liver and almost none in human hepatoma.
