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R G Dennick

Publications and source records attributed to R G Dennick.

14 recordsLinked to original sources
PubMed2005

Developing learning outcomes for an ideal MSc course in sports and exercise medicine.

OBJECTIVE: To develop learning outcomes for an ideal MSc in sports and exercise medicine. METHODS: Twenty nine learning outcomes were developed based on the learning outcomes, aims, and objectives of current sports medicine courses, occupational standards, and other related data. Using a Likert scale, the opinion of MSc/Dip course directors in the United Kingdom, Ireland, Australia, New Zealand, and South Africa as well as teachers, graduates, and students of the MSc/Dip course at the University of Nottingham were surveyed. An email questionnaire listing the 29 learning outcomes was sent to the subjects. A mixed reminder via email or mail was used. The results were treated as ordinal data, and reliability and internal consistency of the questionnaire was tested using Cronbach's coefficient alpha. RESULTS: Response rates were high (75% course directors, 79%, 54%, and 78% University of Nottingham teachers, graduates, and students respectively). The questionnaire was highly reliable (alpha>0.8). The total scores of all but one of the responders were above the midpoint (>87, possible range 29-145). Most course directors (>80%) agreed or strongly agreed with each of the learning outcomes, except two. Most of the other subjects also agreed or strongly agreed with the learning outcomes, with few exceptions. CONCLUSION: The results suggest that there is a consensus among subjects that the final listed learning outcomes should be included in an ideal MSc in sports and exercise medicine.

Attitude of Health Personnel↗
PubMed1981

Regiospecific attack of nitrogen and sulfur nucleophiles on quinones derived from poison oak/ivy catechols (urushiols) and analogues as models for urushiol-protein conjugate formation.

Attempts to characterize potential biologically important covalent interactions between electrophilic quinones derived from catechols present in poison oak/ivy (urushiol) and biomacromolecules have led to the analysis of model reactions involving sulfur and amino nucleophiles with 3-heptadecylbenzoquinone. Characterization of the reaction products indicates that this quinone undergoes regiospecific attack by (S)-N-acetylcysteine at C-6 and by 1-aminopentane at C-5. The red solid obtained with 1-aminopentane proved to be 3-heptadecyl-5-(pentylamino)-1,2-benzoquinone. Analogous aminobenzoquinones were obtained with the quinones derived from the 4- and 6-methyl analogues of 3-pentadecylcatechol. All three adducts absorbed visible light at different wavelengths. When the starting catechols were incubated with human serum albumin almost identical chromophores were formed. These results establish that cathechols responsible for the production of the poison oak/ivy contact dermatitis in humans undergo a sequence of reactions in the presence of human serum albumin that lead to covalent attachment of the catechols to the protein via carbon-nitrogen bonds. Estimations of the extent of this binding indicate that, at least with human serum albumin, the reaction is quantitative.

Catechols↗
PubMed1981

Characteristics of two anti-tumour monoclonal antibody preparations.

Monoclonal antibodies directed against one spontaneously arising rat mammary carcinoma and a human osteogenic sarcoma have been prepared following the fusion of spleen cells from appropriately immunised donors with mouse myeloma cells. The characteristics of these antibodies have been analysed and methods for their purification have been developed using immunoadsorption chromatography or by utilising their affinity for Sepharose-linked Protein A. The use of these antibodies for the identification, characterisation and isolation of their target tumour antigenic structures is described.

Animals↗
PubMed1979

Modification of the immunogenicity and antigenicity of rat hepatoma cells. I. Cell-surface stabilization with glutaraldehyde.

gamma-Irradiated rat hepatoma cells are immunogenic in syngeneic WAB/Not rats, so that immunized animals are protected against tumour-cell challenge and circulating tumour-specific antibody is produced. Treatment of the immunizing cells with glutaraldehyde at concentrations of 0.001% or greater for 30 min rendered these cells non-protective in tumour-rejection tests and no longer able to induce significant formation of specific antibody. However, tumour-specific antigens were shown to be expressed upon treated cells; they specifically bound tumour-specific antibody from syngeneic immune sera assessed in indirect membrane-immunofluorescence tests. Also, these cells specifically absorbed antibody from immune or tumour-bearer sera, as demonstrated in the indirect membrane-immunofluorescence test or a complement-dependent 51Cr-release test. Alloantigen expression was not influenced by glutaraldehyde treatment, although glutaraldehyde-treated hepatoma cells failed to induce alloantibody formation in KX/Not rats. Polyacrylamide-gel electrophoresis of treated cells, surface-labelled with 125I, indicated that extensive cross-linking of the surface protein occurred as a result of glutaraldehyde treatment. The present findings establish that although the expression of a tumour-specific antigen is necessary for the induction of immuno-protection against tumour-cell challenge, this alone is not a sufficient condition for eliciting tumour immunity.

Animals↗
PubMed1979

Modification of the immunogenicity and antigenicity of rat hepatoma cells. II. Mild heat treatment.

I.p. immunization with gamma-irradiated hepatoma cells induces resistance to s.c. tumour-cell challenge in syngeneic WAB/Not rats. Mild heat treatment of these cells (greater than 41 degrees C for 30 min) destroyed this immunoprotective effect, but did not abolish tumour-specific antibody production in treated rats. The binding of syngeneic and alloantibodies to surface antigens expressed on hepatoma cells was unaffected by heat treatment. Thus, heat-treated gamma-irradiated hepatoma cells retain a serologically defined tumour-specific antigen but are unable to elicit immunoprotection. By examining the incorporation of radioactive precursors into DNA, RNA and protein in heat-treated cells, it was determined that above 41 degrees C there was a significant decrease in metabolic activity. It is postulated that for the effective induction of transplantation immunity to tumours, tumour-specific antigens should be present on the surface membranes of a metabolically active cell. This hypothesis accounts for the absence or marked reduction of immunoprotection induced by inviable or glutaraldehyde-treated cells, isolated cell membranes and soluble tumour extracts which retain serologically defined tumour-specific antigens.

Animals↗
PubMed1977

Purification and immunochemical characterization of monoamine oxidase from rat and human liver.

1. Monoamine oxidase from rat and human liver was purified to homogeneity by the criterion of polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate. 2. The enzyme activity was extracted from mitochondrial preparations by Triton X-100. The enzyme was purified by (NH4)2SO4 fractionation followed by chromatography on DEAE-cellulose, Sepharose 6B, spheroidal hydroxyapatite, and finally chromatography on diazo-coupled tyramine-Sepharose. 3. Distinct differences occur in the chromatographic behaviour of the two enzymes on both DEAE-cellulose and spheroidal hydroxyapatite. 4. It is unlikely that the purification of the enzymes on tyramine-Sepharose is due to affinity chromatography and reasons for this are discussed. 5. The purified enzymes did not oxidize-5-hydroxytryptamine and the relative activities of the enzymes with benzylamine were increased approx. 1.25-fold compared with the enzyme activities of mitochondrial preparations. 6. Immunotitration of enzyme activity in extracts of mitochondrial preparations from rat liver was carried out with 5-hydroxytryptamine, tyramine and benzylamine. The enzyme activities were completely immunoprecipitated by the same volume of antiserum. Similar results were obtained with the antiserum to the enzyme from human liver.

Animals↗