Please use this identifier to cite or link to this item: https://repositorio.unifesp.br/handle/11600/43451
Title: ALTERATIONS INDUCED BY PENICILLIN IN THE PROTEIN PROFILE AND CELL STRUCTURE OF GROUP G-STREPTOCOCCUS
Authors: Decastro, ACD
Meirelles, MNL
Santos, AHD
Vieira, V. V.
Leite, LHR
Travassos, Luiz Rodolpho [UNIFESP]
Vermelho, A. B.
Universidade Federal de São Paulo (UNIFESP)
FIOCRUZ MS
Universidade Federal do Rio de Janeiro (UFRJ)
Issue Date: 1-May-1994
Publisher: Springer
Citation: Current Microbiology. New York: Springer Verlag, v. 28, n. 5, p. 269-273, 1994.
Abstract: We investigated the effect of a subminimal concentration of penicillin on the ultrastructure and protein profile of Group G streptococci. In cells treated with penicillin (1/3 MIC), the protein content increased by 50%, and several protein bands with a molecular mass of 14-70 kDa were detected. In the hydrophilic phase, carbohydrate-containing proteins were detected by PAS staining, and in the hydrophobic phase, a group of proteins that reacted strongly with homologous antisera were observed. In terms of cell structure, Triton X-114 extraction was found to induce alterations in the cross wall of untreated cells. In bacteria treated with penicillin but not extracted with Triton X-114, the cell wall was observed to detach itself, and regions with reduced amounts of cellular material appeared in the cytoplasm. After Triton-X114 extraction, these penicillin-treated cells exhibited profound morphological changes, leading in some cases to lysis.
URI: http://repositorio.unifesp.br/11600/43451
ISSN: 0343-8651
Other Identifiers: http://dx.doi.org/10.1007/BF01573204
Appears in Collections:Artigo

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.