作者: Mitsuko T. Laforet , Jane B. Butterfield , Joseph B. Alpers
DOI: 10.1016/0003-9861(74)90154-4
关键词: Human erythrocytes 、 Biosynthesis 、 Enzyme 、 Mutase activity 、 Phosphoglycerate mutase 、 Diphosphoglycerate 、 Mutase 、 Biology 、 Muscle enzyme 、 Biochemistry 、 Biophysics 、 Molecular biology
摘要: Abstract Monophosphoglycerate mutase from rabbit muscle catalyzes the biosynthesis of 2,3-diphosphoglycerate 1,3-diphosphoglycerate and 3-phosphoglycerate. Net synthesis occurs out proportion to what would be expected operation overall monophosphoglycerate reaction. 1,3-Diphosphoglycerate also stimulates reaction, which provides additional proof that it interacts with this enzyme. When is treated at 55 °C in mild acid, action ability generate are lost about same extent. It proposed displaces regenerates enzyme phospho- form. In order assess whether reaction contributes production red cells, was partially purified human erythrocytes. The ammonium sulfate fraction richest shows many properties enzyme, presence readily generates 2,3-diphosphoglycerate. However, largely retained upon heating, despite severe loss activity. This contrasts behavior raises possibility either does not contribute substantially erythrocytes or can indeed produce but abilities catalyze selectively dissociated by heat treatment.