Abstract
Summary 3-Phosphoglycerate kinase from Turbatrix aceti , when partially pure, shows a molecular weight which varies from 43,000 to 160,000 on columns of Sephadex G-150 or G-100, depending upon the eluting buffer and its ionic strength. The pure enzyme has an unchanging molecular weight of 43,000 ± 2,000. Similar shifts of molecular weight have been observed in partially purified preparations of phosphoglycerate kinase from rat liver and from yeast. A low molecular weight factor, presumably a protein, appears to be associated with partially pure preparations of the nematode enzyme. This material is removed from the enzyme by ion-exchange chromatography and is responsible for the aggregation of phosphoglycerate kinase molecules.
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