The purification and properties of diphosphoglycerate mutase from human erythrocytes.

摘要: Diphosphoglycerate mutase has been purified from the red blood cells of rabbits and humans. The enzyme is found only in soluble fraction human cell hemolysates at an average level 0.93 unit per ml packed cells. stoichiometry verified as: 1,3-PGA + 3-PGA → 2,3-PGA where PGA phosphoglyceric acid. kinetic studies with indicate Km values 0.53 µ M for 1,3-diphosphoglycerate 1 to 1.5 3-phosphoglycerate. 2,3-Diphosphoglycerate a competitive inhibitor Ki 0.85 ; it noncompetitive Inorganic phosphate inhibits competitively 3-phosphoglycerate 314 . 1,3-diphosphoglyceric acid independent An ordered bimolecular reaction proposed which combines free enzyme, followed by combination form ternary complex. After conversion products, released before 2,3-diphosphoglycerate. inhibited sulfhydryl reagents fractions require addition mercaptoethanol optimal activity. Phosphoglycolic stimulatory levels below 0.4 m inhibitory higher levels. 2-Phosphoglycerate activator reaction. It decreases increases over-all activity enzyme. 2-Phosphoglyceric also acts as acceptor produce