Purification and Properties of Crystalline 2-Phospho-d-Glycerate Hydro-Lyase from Human Muscle

Abstract

1 The purification and crystallization of 2-phospho-d-glycerate hydro-lyase from human skeletal muscle is described. 2 Preparations of the crystalline enzyme were found to be homogenous as examined in free boundary and gel electrophoresis. Chromatography on Sephadex G 75 and TEAE-cellulose revealed only one component. 3 The sedimentation constant was found to be 5.97×10−13 sec, the diffusion constant 5.6×10−7 cm2/sec and the intrinsic viscosity 4.10 ml/g. The molecular weight calculated from these data was found to be 95,000 ± 3,000, and the frictional ratio 1.26. 4 The properties of the enzyme are compared with those of phosphopyruvate hydratase from rabbit muscle and yeast.