Purification and Properties of Phosphoribosyl-formylglycineamidine Synthetase of Ehrlich Ascites Tumor Cells

Publisher Website
Google Scholar
Abstract
Phosphoribosyl-formylglycineamidine synthetase was purified 56-fold from Ehrlich ascites tumor cells. The reaction required potassium ion as activator, and a combination of glutamine, magnesium chloride, and potassium chloride protected the enzyme against thermal denaturation. Ammonium ion could replace potassium ion as activator, and could replace glutamine as substrate. Studies with radioactive substrates suggest that the reaction is wholly or partially ping pong; glutamine is converted to glutamate by the free enzyme.

This publication has 0 references indexed in Scilit: