Purification and partial characterization of the exotoxin of Corynebacterium ovis

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Abstract
The toxin from C. ovis [pseudotuberculosis], a phospholipase D (sphinogomyelin phosphodiesterase D) (EC 3.1.4.41) that acts on 2-lysophosphatidylcholine and sphinogomyelins, was purified by about 400-fold to homogeneity as judged by several criteria. A new assay method performed in vitro, based on inhibition by the toxin of erythrocyte lysis by staphylococcal .beta.-hemolysin, was developed to facilitate the purification. The toxin was a basic (pI [isoelectric point]9.1) glycoprotein of MW 14,500 .+-. 1000. The amino acid composition of the toxin was highly reminiscent of that of collagen, since it contained hydroxyproline, hydroxylysine and a high proportion of glycine, but preliminary tests showed no other similarities to collagen or proteins with similar compositions.