Abstract
The oxygen-stable streptococcal hemolysins, which can be induced by a number of diverse substances, have been studied. Differences among these hemolysins have been found in electrophoresis, chromatography, pH stability, and susceptibility to some organic solvents and to an enzyme, RNAase. These properties have in each case been found to characterize the inducing substances as well. In a number of instances it has been found possible to incubate one inducer with the hemolysin induced by another of these agents and then, after appropriate fractionation, to find hemolytic activity in the fraction containing the fresh inducer. These observations suggest that the oxygen-stable streptococcal hemolysins are constituted as carrier-hemolysin complexes, the carriers being the set of molecular species effective as inducers, and the prosthetic group being transferred from one carrier to another under appropriate conditions. After transfer of the hemolytic moiety from a hemolysin molecule which is susceptible to inactivation by a given agent or set of conditions to a carrier which is not itself significantly affected by this agent, the new, derived, hemolysin has been found not to be inactivated by the agent. The hemolysins of this group can thus be inactivated by enzymatic attack on the prosthetic group, or by hydrolysis or deformation of the postulated carrier molecule.
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Selected References
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- BERNHEIMER A. W. Formation of a bacterial toxin (streptolysin S) by resting cells. J Exp Med. 1949 Nov;90(5):373–392. doi: 10.1084/jem.90.5.373. [DOI] [PMC free article] [PubMed] [Google Scholar]
- BERNHEIMER A. W. Stabilization of streptolysin S by potassium ions. J Exp Med. 1950 Aug;92(2):129–132. doi: 10.1084/jem.92.2.129. [DOI] [PMC free article] [PubMed] [Google Scholar]
- CARLSON L. A. Chromatographic separation of serum lipoproteins on glass powder columns. Description of the method and some applications. Clin Chim Acta. 1960 Jul;5:528–538. doi: 10.1016/0009-8981(60)90064-4. [DOI] [PubMed] [Google Scholar]
- GINSBURG I., GROSSOWICZ N. A cell-bound hemolysin of group A streptococci. Bull Res Counc Isr Sect E Exp Med. 1958 Dec;7E:237–246. [PubMed] [Google Scholar]
- GINSBURG I., HARRIS T. N., GROSSOWICZ N. OXYGEN-STABLE HEMOLYSINS OF GROUP A STREPTOCOCCI. I. THE ROLE OF VARIOUS AGENTS IN THE PRODUCTION OF THE HEMOLYSINS. J Exp Med. 1963 Dec 1;118:905–917. doi: 10.1084/jem.118.6.905. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HUMPHREY J. H. The nature of antistreptolysin S in the sera of man and of other species; the lipoprotein properties of antistreptolysin S. Br J Exp Pathol. 1949 Oct;30(5):365–375. [PMC free article] [PubMed] [Google Scholar]
- PETERSON E. A., CHIAZZE E. A. Some experimental factors in the gradient chromatography of serum proteins. Arch Biochem Biophys. 1962 Oct;99:136–147. doi: 10.1016/0003-9861(62)90256-4. [DOI] [PubMed] [Google Scholar]
- STOLLERMAN G. H., BERNHEIMER A. W., MacLEOD C. M. The association of lipoproteins with the inhibition of streptolysin S by serum. J Clin Invest. 1950 Dec;29(12):1636–1645. doi: 10.1172/JCI102408. [DOI] [PMC free article] [PubMed] [Google Scholar]