The Journal of Experimental Medicine
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The Journal of Experimental Medicine, Vol 118, 905-917, Copyright © 1963, by The Rockefeller Institute

ARTICLE

OXYGEN-STABLE HEMOLYSINS OF GROUP A STREPTOCOCCI : I. THE ROLE OF VARIOUS AGENTS IN THE PRODUCTION OF THE HEMOLYSINS



Isaac Ginsburg Ph.D.1, T. N. Harris M.D.1, and Nathan Grossowicz Ph.D.1

1 From The Children's Hospital of Philadelphia, Department of Pediatrics, School of Medicine, University of Pennsylvania, and the Department of Bacteriology, The Hebrew University, Hadassah Medical School, Jerusalem, Israel

The production of oxygen-stable hemolysin in growing and resting Group A streptococci has been induced by RNA, by detergents, and by mammalian blood serum proteins, in the presence of glucose, Mg++, and cysteine. Of the serum proteins, albumin and alpha lipoprotein could act as inducers. In the case of both these serum proteins treatment with trypsin did not affect the capacity to induce hemolysin production, but removal of the bound lipids by alcohol-ether or chloroform-methanol destroyed this property.

In comparisons of the conditions of production and of activity between the hemolysin produced by RNA on one hand and albumin and detergents on the other, some data indicated similarities among the hemolysins, and others, differences. The similarities included similar degrees of temperature dependence for production and equal degrees of inhibition by serum ß lipoprotein. Differences found among these hemolysins included differences between, the rate of production of the RNA hemolysin from that of albumin or detergent hemolysin by both resting and growing streptococci, and the failure of utilization of glucosamine as an energy source for the production of albumin hemolysin, in contrast with that of RNA hemolysin. The fact that the data have in some cases indicated similarities and in other cases differences among the hemolysins raises the question of whether these are different molecular species, or a single hemolysin synthesized by the streptococci via different pathways of metabolism, or complexes of a single hemolytic moiety with various molecular carriers.

 Submitted on May 14, 1963


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