Partial purification and conversion of the particulate-bound diglyceride kinase ofEscherichia coli to a water soluble,detergent free state

Alkali (pH 11.5) treatment of a washed, ammonium sulfate-precipitated residue derived from a triton-X-100 extract of a 30,000 Xg particulate diglyceride kinase preparation ofE. coli converts much of the enzyme to a 100,000 Xg soluble, detergent free state. This procedure improves the enzyme as an analytical tool for the structural analysis of triglycerides, and may be applicable for the solubilization of the many other glyceride- and phosphoglyceride-forming enzymes which have all resisted further purification because of insoluble, particulate properties.