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Biomedical subjects

L Brennan

Publications and source records attributed to L Brennan.

At least 19 recordsLinked to original sources
PubMed1992

An audit of induction of anaesthesia in neonates and small infants using pulse oximetry.

The frequency and severity of hypoxaemia during induction of anaesthesia in neonates and small infants at the Norfolk and Norwich Hospital, a district general hospital, was compared, using pulse oximetry, with that of the nearest specialist hospital, the Queen Elizabeth Hospital for Sick Children in London. There were differences in staffing and the choice of anaesthetic techniques between the hospitals. One third of the patients in both hospitals experienced desaturation of more than 5% (moderate or severe hypoxaemia) at one or more recordings during induction. The highest incidence of hypoxaemia was associated with awake intubation. There was no statistical difference in the incidence or severity of hypoxaemia between the hospitals. In the district general hospital, moderate or severe hypoxaemia of greater than 30 s duration was more likely if an anaesthetist with a regular paediatric operating list was not present at induction (p < 0.01).

Anesthesia, Inhalation↗
PubMed1992

University neonatal centers and level II centers compatibility. Jacksonville experience.

Reported are 10 years experience in the development of a Citywide Neonatal Program in the Jacksonville area, which could be helpful as a model for establishing relationships between academic centers and outside Level II nurseries. The four phases of development are documented. An analysis of the financial impact to the academic program is presented and also an outline of the gain realized by the Department of Pediatrics, University of Florida Health Science Center. The positive results in amalgamation of the neonatal services in Jacksonville have far outweighed any potential harmful effects from competition between an academic center and other private nurseries in the city.

Academic Medical Centers↗
PubMed1991

Affinity-chromatographic purification of sixteen cysteine-substituted maltoporin variants: thiol reactivity and cross-linking in an outer membrane protein of Escherichia coli.

Wild-type and 16 variant maltoporins with site-directed cysteine substitutions at 14 sites were purified by a novel one-step affinity-chromatographic procedure. The trimer stability of purified proteins with C22S, C38S and G103C substitutions was reduced compared to wild-type maltoporin. Quantitative labelling with N-ethyl[14C]maleimide, cross-linking with bifunctional bismaleimides and disulphide formation was used to test the reactivity of cysteines in the folded protein. The maleimide reactivity of the residues was in the order: 152 approximately equal to 153 greater than 265 greater than 30 approximately equal to 103 approximately equal to 120 approximately equal to 154 approximately equal to 382 greater than 57 approximately equal to 146, with the other sites (22, 38, 97, 184) poorly labelled. Only cysteines at 152 or 153 permitted the formation of inter-subunit disulphide bonds suggesting these residues are located within 0.5-0.9 nm of each other in homotrimers of maltoporin. S152C and S153C as well as S154C permitted the formation of inter-subunit cross-links using bifunctional bismaleimides. The cross-linkability and the high reactivity to N-ethylmaleimide of the 150 region was consistent with the current model of the structure of maltoporin in the outer membrane; the reactivity of the other sites is also discussed within the context of this model.

Amino Acid Sequence↗
PubMed1991

Genetic mapping of starch- and lambda-receptor sites in maltoporin: identification of substitutions causing direct and indirect effects on binding sites by cysteine mutagenesis.

Cysteine mutagenesis was used to test the proximity of 16 residues to protein-ligand interaction sites in maltoporin (LamB protein). LamB protein with additional cysteines was incorporated into the outer membrane of Escherichia coli except with a Ser-30----Cys substitution. Phage Lambda and starch binding was assayed before and after incubation of mutants with six thiol-specific reagents. Four categories of mutation were recognized on the basis of phenotype and modification for each of the Lambda- and starch binding sites. The thiol modification experiments helped to clarify whether the phenotype of a mutation was due to a substitution at the binding site or an indirect perturbation of the structure. This study suggests that the cysteine mutagenesis/thiol modification approach may be usefully applied to the operational mapping of surface-accessible binding sites or epitopes.

Bacterial Outer Membrane Proteins↗
PubMed1990

Simultaneous flow cytometric measurements of cytoplasmic Ca++ and membrane potential changes upon FMLP exposure as HL-60 cells mature into granulocytes: using [Ca++]in as an indicator of granulocyte maturity.

Treatment of human leukemic HL-60 cells with N,N-dimethylformamide (DMF) induces them to mature until they reach granulocytoid morphology 3-6 d later. We have reported a maturation-dependent ability of these cells to respond to phorbol myristate acetate (PMA), as evaluated by membrane depolarization and by oxidative burst product formation (Newburger et al.: J. Biol. Chem. 259,3771, 1984). More recently we have attempted to develop techniques for simultaneous evaluation of these parameters during HL-60 cell maturation. Here, we compare the cytoplasmic [Ca++] and membrane potential changes elicited by the chemotactic peptide fMLP via simultaneous measurement of individual cells in a fluorescence-activated cell sorter (FACS), as done previously for mature granulocytes (Lazzari et al.: J. Biol. Chem. 261,9710, 1986). The stimulus-induced [Ca++]in changes are detected with the fluorescent probe Indo-1 and reproducibly increase in magnitude for a subpopulation of cells as the cells mature into granulocytes. Ca++ responsiveness to formyl peptide is restricted to a subpopulation of HL-60 granulocytes which expresses receptors for chemotactic peptide and consistently increases in magnitude (in response to the same concentration of agonist) with maturation. In contrast, there is less consistency in the direction or magnitude of membrane potential changes elicited under the same circumstances from the same maturing HL-60 cells.

Calcium↗
PubMed1989

Surgical glove failure rate.

Surgical gloves were collected after day-time operations for a 4-week period. Glove punctures were located by inflating each glove with compressed air and immersing the inflated glove in water. During the period of the study 681 surgical operations were performed. A total of 3790 gloves was collected, 334 gloves (8.8%) had perforations at the end of the surgical procedure. Defects occurred in one or more gloves in 32.0% of all operations.

Equipment Failure↗
PubMed1987

Spectrum and mode of action of azithromycin (CP-62,993), a new 15-membered-ring macrolide with improved potency against gram-negative organisms.

The macrolide antibiotic azithromycin (CP-62,993; 9-deoxo-9a-methyl-9a-aza-9a-homoerythromycin A; also designated XZ-450 [Pliva Pharmaceuticals, Zagreb, Yugoslavia]) showed a significant improvement in potency against gram-negative organisms compared with erythromycin while retaining the classic erythromycin spectrum. It was up to four times more potent than erythromycin against Haemophilus influenzae and Neisseria gonorrhoeae and twofold more potent against Branhamella catarrhalis, Campylobacter species, and Legionella species. It had activity similar to that of erythromycin against Chlamydia spp. Azithromycin was significantly more potent versus many genera of the family Enterobacteriaceae; its MIC for 90% of strains of Escherichia, Salmonella, Shigella, and Yersinia was less than or equal to 4 micrograms/ml, compared with 16 to 128 micrograms/ml for erythromycin. Azithromycin inhibited the majority of gram-positive organisms at less than or equal to 1 micrograms/ml. It displayed cross-resistance to erythromycin-resistant Staphylococcus and Streptococcus isolates. It had moderate activity against Bacteroides fragilis and was comparable to erythromycin against other anaerobic species. Azithromycin also demonstrated improved bactericidal activity in comparison with erythromycin. The mechanism of action of azithromycin was similar to that of erythromycin since azithromycin competed effectively for [14C]erythromycin ribosomebinding sites.

Anti-Bacterial Agents↗
PubMed1986

Educating Martha.

Explore the source record for details and available documents.

Child, Preschool↗
PubMedDate not supplied

Sulbactam/ampicillin: in vitro spectrum, potency, and activity in models of acute infection.

More than 90% of community hospital-isolated strains of Staphylococcus (including methicillin-resistant isolates), Streptococcus, Haemophilus, Neisseria, Branhamella, Bacteroides, Escherichia coli, Klebsiella, Enterobacter aerogenes, Proteus, and Acinetobacter calcoaceticus were inhibited by the sulbactam/ampicillin (1:2) combination at concentrations of 8 micrograms/16 micrograms per ml. The peak serum level from a 15-min infusion of 1 g/2 g of sulbactam/ampicillin is more than seven times this 90% end point. Excellent bactericidal activity was demonstrated against ampicillin-resistant isolates. Ampicillin-resistant strains did not develop resistance to sulbactam/ampicillin when they were serially transferred in the presence of sublethal concentrations of the combination. In mice the combination was active against a variety of acute, fatal infections produced by ampicillin-resistant bacterial isolates, including methicillin-resistant strains of Staphylococcus aureus and mixed anaerobes. The in vitro and in vivo properties of sulbactam/ampicillin, coupled with its reliable pharmacokinetic performance, appear to make the combination ideally suited for the treatment of polymicrobial (aerobe-anaerobe) infections.

Acute Disease↗