The mode of action of highly punned beta hemolysin derived from the R-1 strain of Staphylococcus aureus has been investigated. Sphingomyelin was absent from lipid extracts of sheep erythrocytes treated with beta hemolysin when compared to normal cells. A correlation was also established between the sphingomyelin content of other erythrocyte species and their sensitivity to beta hemolysin. Further investigations revealed that sphingomyelin is hydrolyzed to yield phosphorylcholine and N-acyl sphingosine. Thus, the mode of action of the beta hemolysin is like that of phospholipase C. Various phosphate compounds other than sphingomyelin, including RNA, glycerophosphate, phenyl-phosphate, phosphatidylethanolamine, and phosphatidylcholine were tested as substrates, but virtually no hydrolysis was observed. In contrast with the results of other workers, R-1 beta hemolysin did not release detectable amounts of carbohydrate from staphylococcal cell walls.
No takes yet. Share an insight, caveat, or question.
Wiseman et al. (1967) studied this question.
Synapse has enriched 5 related papers. Consider them for comparative context: