ULTRACENTRIFUGE, ELECTROPHORESIS, AND VISCOSITY STUDIES ON CRYSTALLINE PYROPHOSPHATASE

Abstract

Ultracentrifuge and electrophoresis studies on one preparation of crystalline pyrophosphatase showed the presence of one major component which accounted for more than 90 per cent of the protein. Combination of viscosity, diffusion, and ultracentrifuge data leads to a model of low asymmetry with an anhydrous molecular weight of about 60,000.