Phosphatidyl inositol-specific phospholipase C from Clostridium novyi type A

Abstract

From the culture broth of Clostridium novyi type A, phosphatidyl inositol-specific phospholipase C was separated from the major part of phospholipase C (γ-toxin) which hydrolyzes phosphatidyl choline, phosphatidyl ethanolamine, and sphingomyelin. Sodium deoxycholate stimulated the activity of phosphatidyl inositol phospholipase C. The concentration of sodium deoxycholate for maximal stimulation was 0.2% with 2 mm phosphatidyl inositol. Divalent cations (Mg2+, Ca2+, and Zn2+) were rather inhibitory above 10-3 m. Phosphatidyl inositol phospholipase C was not inhibited by EDTA or o-phenanthroline. When phosphatidyl inositol phospholipase C was incubated with rat liver slices, not only alkaline phosphatase but also 5′-nucleotidase was liberated into the soluble fraction. © 1978.