Abstract
Electron microscopic observations of Streptococcus pyogenes (strain S43, type 6) treated with trypsin and cetyltrimethylammonium bromide (Cetab) are presented. The concentration of trypsin necessary to remove the M protein antigen was shown to bring about a partial digestion of the cells. The cell protoplasm and protoplasmic membrane were affected. No microscopic changes appeared in the cell wall. Cetab did not alter the appearance of the cells. Both trypsin and detergent altered the permeability of the cell so that citrulline and carbamylphosphate were metabolized. Cells exhibiting enzyme activity on these substrates after Cetab treatment were characterized by the release of lysine, glutamic acid, nucleic acid, and other cellular material. Enzymes responsible for the metabolism of arginine, citrulline, and carbamylphosphate were shown to reside in the cell protoplasm. Cells which had lost their viability after Cetab treatment still possessed the ability to utilize the latter substrates. Under similar conditions the metabolism of glucose did not occur. Normal cells were shown to possess the ability to fluoresce in the presence of a dye. The intensity of the fluorescence was reduced by trypsin treatment.
Full Text
The Full Text of this article is available as a PDF (932.7 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- HESS E. L., SLADE H. D. An electrophoretic examination of cell-free extracts from various serological types of group A hemolytic streptococci. Biochim Biophys Acta. 1955 Mar;16(3):346–353. doi: 10.1016/0006-3002(55)90237-7. [DOI] [PubMed] [Google Scholar]
- Lancefield R. C. STUDIES ON THE ANTIGENIC COMPOSITION OF GROUP A HEMOLYTIC STREPTOCOCCI : I. EFFECTS OF PROTEOLYTIC ENZYMES ON STREPTOCOCCAL CELLS. J Exp Med. 1943 Dec 1;78(6):465–476. doi: 10.1084/jem.78.6.465. [DOI] [PMC free article] [PubMed] [Google Scholar]
- SALTON M. R. Cell structure and the enzymic lysis of bacteria. J Gen Microbiol. 1953 Dec;9(3):512–523. doi: 10.1099/00221287-9-3-512. [DOI] [PubMed] [Google Scholar]
- SALTON M. R. Studies of the bacterial cell wall. IV. The composition of the cell walls of some Gram-positive and Gram-negative bacteria. Biochim Biophys Acta. 1953 Apr;10(4):512–523. doi: 10.1016/0006-3002(53)90296-0. [DOI] [PubMed] [Google Scholar]
- SHARP J. T., HIJMANS W., DIENES L. Examination of the L forms of group A streptococci for the group-specific polysaccharide and M protein. J Exp Med. 1957 Feb 1;105(2):153–159. doi: 10.1084/jem.105.2.153. [DOI] [PMC free article] [PubMed] [Google Scholar]
- SLADE H. D. Hydrolysis of arginine by soluble enzymes of Streptococcus faecalis. Arch Biochem Biophys. 1953 Jan;42(1):204–211. doi: 10.1016/0003-9861(53)90253-7. [DOI] [PubMed] [Google Scholar]
- SLADE H. D., VETTER J. K. Studies on Streptococcus pyogenes. I. Observations on the microscopical and biological aspects of the disintegration and solubilization of a type 6 strain by sonic oscillation. J Bacteriol. 1956 Feb;71(2):236–243. doi: 10.1128/jb.71.2.236-243.1956. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Swift H. F., Wilson A. T., Lancefield R. C. TYPING GROUP A HEMOLYTIC STREPTOCOCCI BY M PRECIPITIN REACTIONS IN CAPILLARY PIPETTES. J Exp Med. 1943 Aug 1;78(2):127–133. doi: 10.1084/jem.78.2.127. [DOI] [PMC free article] [PubMed] [Google Scholar]