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Biomedical subjects

R E Thompson

Publications and source records attributed to R E Thompson.

At least 109 records · Page 6Linked to original sources
PubMed1978

The use of a fluorescence typing method in an epidemiological study of Klebsiella infection in a London hospital.

The fluorescent antibody technique was used to investigate an epidemic of Klebsiella infection in a urological ward and to trace the probable source to a contaminated sink in the treatment room. It was also shown that cross infections by particular capsular types were very common within each ward. Certain types of Klebsiella occurred in cut flower water but could not be associated with the types infecting the patients. Antibiotic resistance patterns within one capsular type were found to vary whether the type was from different sources in one patient or from different patients in the same ward. One capsular type was observed to develop resistance to increasing numbers of antibiotics over a 3-year period. This was probably due to the acquisition of R-plasmids. There also appeared to be a relation between capsular type and the site of infection. The frequency of Klebsiella infections in the urological wards dropped significantly after up-grading the treatment room, improving catheter storage and reducing ampicillin use.

Anti-Bacterial Agents↗
PubMed1978

Evaluating quality isn't worth the cost.... unless.

The uses for valid patient care data are increasing. However, evaluating quality of care must be done in a more efficient, productive manner if the cost is ever to be justified. Five suggestions are provided to develop better study methods for this purpose.

Efficiency↗
PubMed1978

Six flaws revealed: how to make your audit/MCE studies more meaningful.

A study that lacks a definite design lacks direction and is defeated before it starts. Careful study design, however, is not the only indication of a successful audit. Approaching variation analysis in a positive rather than punitive manner enhances the committee's ability to recognize important findings and discover imaginative uses for audit data. When problems in care are revealed through evaluation activities, the committee must make recommendations that are appropriate to the causes of the problem and that can be readily implemented. An audit committee that discharges these responsibilities will produce a study that should surely yield informative data. The committee's ultimate goal--improved patient care--can not be far behind.

Analysis of Variance↗
PubMed1977

Association of factor XI and high molecular weight kininogen in human plasma.

Factor XI and high molecular weight kininogen were found associated in normal human plasma at mol wt 380,000 as assessed by gel filtration on Sephadex G-200. The molecular weight of Factor XI in high molecular weight kininogen-deficient plasma was 175,000, the same value obtained for purified Factor XI. When high molecular weight kininogen-deficient plasma was reconstituted with purified high molecular weight kininogen, all of the Factor XI was then found at mol wt 380,000. Complex formation was also demonstrable upon incubation of Factor XI and highly purified high molecular weight kininogen. This complex was distinct from the prekallikrein-high molecular weight kininogen complex; thus high molecular weight kininogen forms bimolecular complexes with either Factor XI or prekallikrein but does not form a trimolecular complex that includes both Factor XI and prekallikrein. Neither Hageman factor nor plasminogen were found associated with high molecular weight kininogen; binding to high molecular weight kininogen appeared to be a specific property of the Hageman factor substrates.

Centrifugation↗
PubMed1977

Isolation and characterization of canine secretory immunoglobulin M.

Canine secretory immunoglobulin M, isolated from both colostrum and bronchial secretions, contained the unique glycoprotein bound secretory component. The presence of this extra subunit accounted for the differences in size, quaternary structure, and antigenicity observed upon comparison of secretory immunoglobulin M with its serum counterpart. Approximately 90% of the isolated secretory immunoglobulin M contained covalently bound secretory component while, in the remainder of the population, secretory component was loosely attached and easily dissociated from the immunoglobulin. Following peptide bond cleavage with cyanogen bromide, the release of bound secretory component and J chain from secretory immunoglobulin M was not detected. Because cyanogen bromide cleavage of secretory immunoglobulin A results in the release of these subunits, differences in the primary structure of secretory immunoglobulin M and secretory immunoglobulin A must exist around the binding sites for secretory component and J chain.

Animals↗
PubMed1976

Rat liver cytoplasmic glucose-6-phosphate dehydrogenase. Steady-state kinetic properties and circular dichroism.

Steady-state kinetic studies including initial velocity, NADPH product inhibition, dead-end inhibition, and combined dead-end and product inhibition measurements with purified rat liver glucose-6-phosphate dehydrogenase indicate a sequential and obligatory addition of substrates in the order of NADP+, glucose-6-P for the catalytic pathway at pH 8.0. Although instability of 6-phosphoglucono-delta-lactone precluded product inhibition experiments which might directly exclude an enzyme-6-phosphoglucono-delta-lactone complex, the absence of an enzyme-glucose-6-P complex suggests that the enzyme-lactone product is unlikely and the release of products is also ordered, with NADPH released last. Consideration of the kinetic constants (Ka = 2.0 muM, Kiq = 13 muM) and cellular concentration of the substrates and products suggests extensive inhibition of the enzyme in vivo and control by the NADPH/NADP+ ratios. Circular dichroism spectra of the enzyme in 20 mM phosphate buffer at pH 7.0 and 25 degrees C indicate 51% helix and 33% pleated sheet structures which is considerably different from results (14% helix) with yeast enzymes.

Animals↗