PURIFICATION OF THE SOLUBLE HEMOLYSINS OF LISTERIA MONOCYTOGENES.
Jenkins, E. M. (Tuskegee Institute, Tuskegee, Ala.), A. N. Njoku-Obi, and E. W. Adams. Purification of the soluble hemolysins of Listeria monocytogenes. J. Bacteriol. 88:418-424. 1964.-A method is described for obtaining relatively purified hemolysin preparations from both virulent and avirulent strains of Listeria monocytogenes. These hemolysins are protein in nature as shown by heat lability, nondialyzable properties, precipitation with trichloroacetic acid, and electrophoretic mobility. The hemolysins are antigenic in rabbits as shown by serum neutralization tests. The potency of the purified hemolysin was markedly increased by cysteine, sodium hydrosulfite, and a number of reducing agents. Many of the actions of the purified hemolysin seemed to parallel that of streptolysin O, and certain of these activities could be explained by the "thioldisulfide hypothesis."
D000818:Animals; D001426:Bacterial Proteins; D003545:Cysteine; D006460:Hemolysin Proteins; D008089:Listeria monocytogenes; D010084:Oxidation-Reduction; D011506:Proteins; D011817:Rabbits; D012106:Research; D013301:Streptolysins
D001426:Bacterial Proteins; D006460:Hemolysin Proteins; D011506:Proteins; D013301:Streptolysins; C025964:streptolysin O; D003545:Cysteine
EXPERIMENTAL LAB STUDY; HEMOLYSINS; LISTERIA MONOCYTOGENES; OXIDATION-REDUCTION; RABBITS