1887

Abstract

Surmmary

The substance responsible for lysis of erythrocytes by cultures of designated subtilysin, was purified. It contained a peptide of leucine, aspartic acid, glutamic acid and valine and probably a lipid. Subtilysin was activated by Mg, Mn and Ca. The rate of haemolysis was abruptly increased by chilling the reaction mixture. Haemolysis was inhibited by normal sera; the most inhibitory serum fractions contained α-and -globulins. Haemolysis was inhibited by low concentrations of phosphatidylcholine, phosphatidylinositol, phosphatidic acid and sphingomyelin. Subtilysin possessed antibiotic properties and lysed protoplasts and spheroplasts derived from several bacterial species; subtilysin was identical with surfactin, a peptidelipid from cultures that inhibits fibrin clot formation. Kakinuma and co-workers found surfactin to be a heptapeptide having an -terminal glutamic acid in amide linkage with the carboxyl group of 3-hydroxy-13-methyl-tetradecanoic acid. Surfactin (subtilysin) possesses some properties in common with two other cytolytic agents of bacterial origin, namely, staphylococcal η-toxin and streptolysin S.

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1970-06-01
2022-05-16
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