Biomedical subjects

J Cavanagh

Publications and source records attributed to J Cavanagh.

50 records · Page 3Linked to original sources

PubMed1992

Clinical complaints and their handling: a time for change?

OBJECTIVES: To assess the performance of the hospital complaints procedure for complaints proceeding to peer review and the quality of responses to complainants. DESIGN: Retrospective study of data on clinical complaints proceeding to peer review during 1986-91 from clinical records, correspondence, reports of the complaints investigations, and expert review of written responses to complainants. SETTING: Northern Regional Health Authority, covering three million people. SUBJECTS: All 71 clinical complaints investigated to the third stage of the hospital complaints procedure and a sample of 65 written responses to complainants. MAIN MEASURES: Characteristics, duration, and outcome of complaints; findings of peer review; and quality of written responses at various stages in the procedure as evaluated by an expert panel against eight agreed criteria. RESULTS: The median duration of a complaint investigated through all stages of the procedure was 381 days. The longest median stages were those involving attempted resolution locally (131 days) and in which peer review was being arranged (113 days). More complaints alleging failure of communication were upheld by peer review (46/59, 78%) than those alleging misapplication of clinical skills (20/98, 20%) or failure to initiate appropriate investigations or treatment (8/32, 25%). Written responses commonly fell below the standards agreed by the expert panel. CONCLUSIONS: The hospital complaints procedure takes too long and its final peer review stage may not demonstrate sufficient impartiality. The written responses suggest that criticism is not welcomed as a way of improving service. IMPLICATION: The clinical complaints procedure needs to be reformed to ensure true accountability to patients.

Data Collection↗

PubMed1991

Uniform labeling of a recombinant antibody Fv-fragment with 15N and 13C for heteronuclear NMR spectroscopy.

The expression of functional antibody fragments in Escherichia coli enables a detailed analysis by NMR spectroscopy. This is demonstrated with the uniform labeling of an Fv-fragment (25 kDa) comprising the antigen binding site of an antibody against 2-phenyloxazolone with 15N and 13C. The antigen-complexed Fv-fragment was analysed for a potential assignment by heteronuclear multi-dimensional NMR spectroscopy. For almost all backbone amides 15N/1H crosspeaks and for 80% of them TOCSY crosspeaks were observed. In a 13C-edited-HCCH-2D experiment 17 out of 18 threonine spin-systems were identified. Thus detailed assignments are possible, but some amino acid specific labeling in addition to uniform labeling will be required for complete assignments of Fv-fragments.

Base Sequence↗

PubMed1991

Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis enzyme IIIglc determined by two-dimensional and three-dimensional heteronuclear NMR spectroscopy.

The enzyme IIIglc-like domain of Bacillus subtilis IIglc (IIIglc, 162 residues, 17.4 kDa) has been cloned and overexpressed in Escherichia coli. Sequence-specific assignment of the backbone 1H and 15N resonances has been carried out with a combination of homonuclear and heteronuclear two-dimensional and heteronuclear three-dimensional (3D) NMR spectroscopy. Amide proton solvent exchange rate constants have been determined from a series of 1H-15N heteronuclear single-quantum coherence (HSQC) spectra acquired following dissolution of the protein in D2O. Major structural features of IIIglc have been inferred from the pattern of short-, medium- and long-range NOEs in 3D heteronuclear 1H nuclear Overhauser effect 1H-15N multiple-quantum coherence (3D NOESY-HMQC) spectra, together with the exchange rate constants. IIIglc contains three antiparallel beta-sheets comprised of eight, three, and two beta-strands. In addition, five beta-bulges were identified. No evidence of regular helical structure was found. The N-terminal 15 residues of the protein appear disordered, which is consistent with their being part of the Q-linker that connects the C-terminal enzyme IIIglc-like domain to the membrane-bound IIglc domain. Significantly, two histidine residues, His 68 and His 83, which are important for phosphotransferase function, are found from NOE measurements to be in close proximity at the ends of adjacent strands in the major beta-sheet.

Amides↗

PubMed1989

Complete assignment of the 1H NMR spectrum of a synthetic zinc finger from Xfin. Sequential resonance assignments and secondary structure.

A 25-residue synthetic peptide corresponding to zinc finger 31 of the Xenopus protein Xfin adopts a compact, folded conformation in the presence of zinc. Complete 1H resonance assignments have been made. The peptide contains a helix, beginning as an alpha-helix and ending as a 3(10)-helix, that extends from residue 12 to 23. Several positively charged and polar residues located on this helix are likely to be involved in interactions with DNA. Residues 1-10 appear to adopt a hairpin-like structure.

Amides↗

PubMed1989

Involvement of the MN blood group antigen in shear-enhanced hemagglutination induced by the Escherichia coli F41 adhesin.

An adhesin from Escherichia coli F41 with an apparent subunit molecular weight of 28,000 daltons was isolated by using (NH4)2SO4 precipitation at pH 10 and Sephacryl S-500 gel filtration. The hemagglutination (HA) properties of the native high-molecular-weight adhesin were studied by using a viscometric assay, which provided a quantitative index of the degree of agglutination present as a function of time at a known rate of shear. Shear was found to enhance the degree of agglutination over a 20-min period. A strong, shear-enhanced HA was observed for all donors with the MM or MN blood type studied, but those with the NN blood type showed very little HA. In the microtiter HA assay, the selectivity of the adhesin for MM over NN erythrocytes was found to be dependent on pH and temperature. At 21 degrees C and pH 7.4, there was little difference in HA between the two blood types, but NN cells were progressively more weakly agglutinated than MM cells as the pH or the temperature was increased. Glycophorin A, which bears the M or N determinant, was isolated from individuals with the MM and NN blood types and was shown to be an effective inhibitor of the reaction, with the MM type being the more effective in both microtiter and viscometric assays. Acidic monosaccharides, particularly sialic acid, were also effective inhibitors of HA, although they were less potent on a molar basis than glycophorin. The adsorption isotherm of 125I-labeled adhesin was measured, and the binding was shown to be strongly inhibited by MM glycophorin and somewhat less strongly by NN glycophorin. Collectively, these data strongly suggest that glycophorin AM is a receptor for the F41 adhesin.

Adhesins, Escherichia coli↗

PubMed1977