Advances in Microbial Physiology, Vol. 36 by A.H. Rose, D.W. Tempest (Ed.)

By A.H. Rose, D.W. Tempest (Ed.)

From the experiences of earlier Volumes "This sequence has continuously awarded a well-balanced account of growth in microbial physiology...Invaluable for educating purposes." -AMERICAN SCIENTIST

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All of these studies pointed to a binding-protein dependence. The finding that the oligopeptide permease is encoded by an operon of several genes, similar to that described previously for other shock-sensitive systems, provided strong endorsement for this view (Higgins and Hardie, 1983). However, early studies failed to detect peptide-binding activity among material released by osmotic shock (Cowell, 1974; Payne, 1980a), probably because of the unusually low affinity of the glycine-containing peptides used and the degradative effect of peptidase activity in the shockates.

W. Payne, unpublished results). The protein DppA is amongst the most abundantly produced periplasmic proteins under typical growth conditions, although it is synthesized in smaller amounts than OppA. The dipeptide-binding protein from E. , 1992). 1, respectively. However, when subjected to Edman degradation, these samples gave only a single protein sequence corresponding to the first 33 residues predicted from the nucleotide sequence (Smith, 1992). 1 on IEF. 9. B4). B4) (Tyreman, 1990; Smith, 1992; Blank, 1987).

In oral streptococci, the organism implicated as of greatest significance in the causation of dental canes is Strep. mutans.

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