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J W Dale

Publications and source records attributed to J W Dale.

70 records · Page 4Linked to original sources

Plasmid-determined beta-lactamase indistinguishable from the chromosomal beta-lactamase of Escherichia coli.

A plasmid, derived from a naturally occurring strain of Proteus mirabilis, conferred resistance to cephalosporins, apparently mediated by a beta-lactamase indistinguishable from that determined by the chromosomal gene of Escherichia coli K-12. There was evidence for a recombination event between the wild-type plasmid and a defective F factor (Fsp) in the Escherichia coli K-12 culture in which it was stored.

Cephalosporins↗

Suspected poisoning in children. Study of the incidence of true poisoning and poisoning scare in a defined population in North East Bristol.

The distinction between true and suspected poisoning in children has not been made clear in previous work on childhood poisoning. A study of suspected poisoning in children under 15 years of age in a defined population of North East Bristol from November 1970 to July 1973 carried out by the Health Education Council Medical Research Division included 53,000 child-years at risk. The number of suspected poisonings was 3-4/1000 population aged under 15 years per year, with a higher incidence in younger age groups. Detailed investigation of the circumstances of the accidents carried out by a multidisciplinary team showed that at least 65%, and possibly as many as 78% were poisoning scares and not true poisoning. The evidence used by the casualty doctor and by the parents to diagnose poisoning was explored, and in many cases was circumstantial. Children with fathers in nonmanual occupations were over-represented. This may reflect differences in patterns of utilization behaviour rather than true differences in incidence.

Accidents, Home↗

An inducible beta-lactamase in a strain of Escherichia coli.

The production of beta-lactamase (penicillin/cephalosporin beta-lactam amidohydrolase, E.C.3.5.2.6) was found to be inducible in a clinically isolated strain of Escherichia coli. This is the first report of an inducible beta-lactamase in E. coli. The optimal concentration of inducer was 400 mug/ml of ml of benzylpenicillin, or 800 mug/ml of 6-aminopenicillanic acid. About fiftyfold induction was achieved. Maximum induction took ninety minutes from the time of adding the inducer. Induction was abolished by the presence of chloramphenicol(10 mug/ml). The enzyme has a molecular wieght of 23,000, and is inhibited by rho-chloromercuribenzoate and by iodine. It is active against a wide range of substrates, including cephaloridine and cloxacillin.

Chloramphenicol↗

R-factor-mediated beta-lactamases that hydrolyze oxacillin: evidence for two distinct groups.

The enzymatic and molecular properties of 14 oxacillin-hydrolyzing beta-lactamases, all of them R-factor-specified, were studied, and two distinct groups were found. Four of the enzymes had a molecular weight of 24,000, were active against methicillin, and had an electrophoretic mobility of -0.1 cm/h. Eight enzymes had a molecular weight of 45,000, low activity against methicillin, and an electrophoretic mobility of +0.5 cm/h. The remaining two enzymes were similar to those of the second group in being relatively inactive against methicillin, but their molecular weight was lower (42,000) and their electrophoretic mobility was different (-0.1 cm/h). All the enzymes of both groups were sensitive to inhibition by sodium chloride. The two groups were not completely homogeneous in their enzymatic properties; seven possible subtypes could be recognized.

Ampicillin↗

The purification and properties of the -lactamase specified by the resistance factor R-1818 in Escherichia coli and Proteus mirabilis.

1. The beta-lactamase specified by the R-1818 resistance factor in Escherichia coli was purified 300-fold; the resulting preparation gave a single peak on Sephadex G-100 and a single band on polyacrylamide-gel electrophoresis. 2. The beta-lactamase specified by the same R-factor in Proteus mirabilis was purified over 2000-fold, but was still far from pure. The specific activity of this preparation was one-fifth that of the purified enzyme from E. coli. 3. The two enzymes were shown to be identical as regards substrate specificity, pH optimum, K(m) values and molecular weight. 4. It is suggested that the low beta-lactamase activity of extracts of P. mirabilis (R-1818), about 5% of that from E. coli (R-1818) in crude extracts, could be due to inefficient transcription of the R-factor DNA by Proteus RNA polymerase.

Chromatography, Gel↗

Characterization of the -lactamase specified by the resistance factor R-1818 in E. coli K12 and other Gram-negative bacteria.

1. The amino acid composition of the beta-lactamase from E. coli (R-1818) was determined. 2. The R-1818 beta-lactamase is inhibited by formaldehyde, hydroxylamine, sodium azide, iodoacetamide, iodine and sodium chloride. 3. The K(m) values for benzylpenicillin, ampicillin and oxacillin have been determined by using the R-factor enzyme from different host species. The same values were obtained, irrespective of the host bacterium. 4. The molecular weight of the enzyme was found to be 44600, and was the same for all host species. 5. The relationship of R-1818 and R-GN238 beta-lactamases is discussed.

Amino Acids↗

Some relationships between R-factor and chromosomal -lactamase in Gram-negative bacteria.

1. The beta-lactamases specified by Klebsiella aerogenes 418 and the R-factor R-7268 have been partially purified. 2. The molecular weights of the K. aerogenes strains 418 and 373, Aerobacter cloacae 53, R-7268 and R-TEM beta-lactamases were all about 20000; that of the enzymes from Escherichia coli strains 419 and 214T was about 31000. 3. These enzymes were also compared by means of their K(m) values for benzylpenicillin and ampicillin, and their behaviour on starch-gel electrophoresis. 4. The beta-lactamases specified by the two Klebsiella strains, the Aerobacter strain, and the R-factors R-TEM and R-7268 were found to comprise a broadly similar group. However, within this group, only two enzymes seemed to be identical, namely those specified by the two R-factors. The two E. coli strains produce identical beta-lactamases which are very different from the ;Klebsiella/Aerobacter-type' enzymes.

Ampicillin↗

Restriction fragment length polymorphism analysis of Mycobacterium tuberculosis isolated from patients with pulmonary tuberculosis in northern Tanzania.

Isolates of Mycobacterium tuberculosis from 88 patients with pulmonary tuberculosis in northern Tanzania were subjected to IS6110 restriction fragment length polymorphism (RFLP) analysis. Of 88 isolates, 73 fell into 11 groups of which 9 contained 2-5 isolates. Of 2 large homology groups one, group H (20 isolates), was isolated only from patients resident in the Kilimanjaro region, whereas 79% of isolates from other groups came from this region. A significant association (P = 0.023) was found between another group, M (24 isolates) and isolation from patients of the Masai tribe. The data from this pilot study support the idea that IS6110 RFLP analysis provides information which may be of value in the control of tuberculosis in Africa.

Adolescent↗