Biomaterial Database

Copurification of Leptospira interrogans serovar pomona hemolysin and sphingomyelinase C. 1986

A W Bernheimer, and R F Bey

The hemolytic and sphingomyelinase C activities of supernatants of cultures of Leptospira interrogans serovar pomona tended to copurify when isoelectric fractionation was carried out. Both activities focused primarily at pH 8.1. Considered in conjunction with other circumstantial evidence, the results led to the conclusion that sphingomyelinase C is responsible for hemolysis.

UI	MeSH Term	Description	Entries
D007919	Leptospira	A genus of aerobic, helical spirochetes, some species of which are pathogenic, others free-living or saprophytic.
D010727	Phosphoric Diester Hydrolases	A class of enzymes that catalyze the hydrolysis of one of the two ester bonds in a phosphodiester compound. EC 3.1.4.	Phosphodiesterase,Phosphodiesterases,Hydrolases, Phosphoric Diester
D006460	Hemolysin Proteins	Proteins from BACTERIA and FUNGI that are soluble enough to be secreted to target ERYTHROCYTES and insert into the membrane to form beta-barrel pores. Biosynthesis may be regulated by HEMOLYSIN FACTORS.	Hemolysin,Hemolysins,Hemalysins,Proteins, Hemolysin
D013108	Sphingomyelin Phosphodiesterase	An enzyme that catalyzes the hydrolysis of sphingomyelin to ceramide (N-acylsphingosine) plus choline phosphate. A defect in this enzyme leads to NIEMANN-PICK DISEASE. EC 3.1.4.12.	Sphingomyelin Cholinephosphohydrolase,Sphingomyelin Cleaving Enzyme,Sphingomyelinase,Sphingomyelinase C