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Biomedical subjects

G W Ross

Publications and source records attributed to G W Ross.

At least 73 records · Page 4Linked to original sources
PubMed1981

Isoelectric focusing studies on Mycobacterium chelonei.

Analytical IEF has been used to give a direct visual comparison of beta-lactamases, down to extremely low levels, from very crude intracellular preparations. Identity and non-identity of strains could be proved by the pattern of bands produced by their beta-lactamases. Mycobacterial species gave a variety of beta-lactamase patterns. Identity was established between some strains of M. chelonei. IEF distinguished between enzymes within both the chelonei and abscessus sub-species that could not be differentiated by other methods. This technique could provide a means of identifying the source of a M. chelonei infection.

Child↗
PubMed1979

Competition of beta-lactam antibiotics for the penicillin-binding proteins of Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella aerogenes, Proteus rettgeri, and Escherichia coli: comparison with antibacterial activity and effects upon bacterial morphology.

The competition of a number of beta-lactam morphogenic probes for the penicillin-binding proteins (PBPs) of Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella aerogenes, Proteus rettgeri, and Escherichia coli has been studied. The results indicate that the various gram-negative bacteria have similar, but not identical, PBP patterns and that the individual proteins probably perform similar morphogenic functions as in E. coli K-12. Comparison of the 50% binding concentrations of the compounds for the various PBPs of the five strains with their antibacterial activity indicates that the different antibiotics are excluded to a greater or lesser degree by the outer membrane permeability barrier and that the exclusion is most pronounced in P. aeruginosa.

Anti-Bacterial Agents↗
PubMed1979

Affinities of penicillins and cephalosporins for the penicillin-binding proteins of Escherichia coli K-12 and their antibacterial activity.

The affinities of a range of penicillins and cephalosporins for ther penicillin-binding proteins of Escherichia coli K-12 have been studied, and the results were compared with the antibacterial activity of the compounds against E. coli K-12 and an isogenic permeability mutant. Different penicillins and cephalosporins exhibited different affinities for the "essential" penicillin-binding proteins of E. coli K-12, in a manner which directly correlated with their observed effects upon bacterial morphology. Furthermore, the affinities of the compounds for their "primary" lethal penicillin-binding protein targets showed close agreement with their antibacterial activities against the permeability mutant.

Bacterial Proteins↗
PubMed1976

Inhibition of peptidoglycan cross-linking in growing cells of Escherichia coli by penicillins and cephalosporins, and its prevention by R factor-mediated beta-lactamase.

The degree of peptidoglycan cross-linking has been studied in growing cells of a Dap(-) Lys(-) auxotroph of Escherichia coli K-12 by following the incorporation of [(3)H]diaminopimelic acid into the lysozyme digestion products of crude, isolated peptidoglycan. The percentage of inhibition of cross-linking increases with increasing concentrations of penicillin G, cephaloridine, and cefuroxime. When the R factor R1drd 19 was introduced into the strain by conjugation, it was found that the type IIIa, beta-lactamase specified by the plasmid was able to protect the cross-linking target against inhibition by penicillin G but not against cephaloridine, even though the beta-lactamase hydrolyzes this substrate 50% faster than penicillin G. Cefuroxime, which is completely resistant to hydrolysis by the type IIIa beta-lactamase, inhibited the peptidoglycan cross-linking target in both the R(+) and R(-) variants of the assay strain. A mutant plasmid, R1drd19amp2, which specified no type IIIa beta-lactamase synthesis, could not provide protection of the cross-linking target against penicillin G. The significance of these results, in relation to the ability of the antibiotics to pass the permeability barrier of the bacterial envelope, is discussed.

Amidohydrolases↗
PubMed1975

The use of analytical isoelectric focusing for detection and identification of beta-lactamases.

BETA-Lactamases (EC. 3.5.2.6) from strains of Gram-negative bacteria have been studied using analytical isoelectric focusing. This permits a visual comparison of the patterns of beta-lactamase bands produced by enzymes from different organisms. Purification of crude intracellular preparations is unnecessary and the technique is sufficiently sensitive to demonstrate beta-lactamase in mutants previously reported to lack the enzyme. R that have not been distinguished from one another biochemically or immunologically can be differentiated by isoelectric focusing. Conversely, the enzymes specified by the R factors RTEM, R1 and RGN14, with identical isoelectric focusing patterns have the same biochemical properties. Chromosomal and R-factor-mediated beta-lactamases from single strains have been separated and their identities confirmed by immunoisoelectric focusing. R factor-mediated enzymes gave identical isoelectric focusing patterns irrespective of the host strain. Isoelectric focusing can therefore be used to observe the transfer of beta-lactamases carried by R factors.

Amidohydrolases↗
PubMed1972

Comparison of the substrate specificities of the -lactamases from Klebsiella aerogenes 1082E and Enterobacter cloacae P99.

A potent beta-lactamase (EC 3.5.2.6) produced by a strain of Klebsiella aerogenes (K. pneumoniae), 1082E, isolated from a hospital patient, has been examined. Its properties were different from those of most gram-negative beta-lactamases previously reported. The enzyme has been partly purified, and its activity against a range of substrates has been compared with that of the enzyme from Enterobacter cloacae (Aerobacter cloacae) P99. The K. aerogenes enzyme, although predominantly a penicillinase, had a wide range of specificity. In addition to hydrolyzing the cephalosporins, it attacked the normally beta-lactamaseresistant compounds methicillin and cloxacillin as well as cephalosporin analogues with the same acyl substituents. The results obtained with the E. cloacae enzyme confirmed its cephalosporinase activity and showed that, unlike the enzyme from K. aerogenes, it was relatively inactive against the penicillins.

Ampicillin↗