Coyette, Jaques and Ghuysen, Jean-Marie and Fontana, Roberta (1978) Solubilization and isolation of the membrane-bound dd-carboxypeptidase of Streptococcus faecalis ATCC 9790. European Journal of Biochemistry, Vol. 88 (1), p. 297-305. eISSN 1432-1033. Article.
Full text not available from this repository.
Streptococcus faecalis ATCC 9790 possesses six membrane-bound, penicillin-binding proteins. That numbered 6 (Mr 43000) is the most abundant one and is the dd-carboxypeptidase studied previously. The enzyme has been solubilized and purified to the stage where one single protein band can be detected by gel electrophoresis. The purification procedure does not alter the properties that the enzyme exhibits when it is membrane-bound. The dd-carboxypeptidase itself may be a killing target for penicillin in S. faecalis.
I documenti depositati in UnissResearch sono protetti dalle leggi che regolano il diritto d'autore
Repository Staff Only: item control page