Biomedical subjects

C M Wells

Publications and source records attributed to C M Wells.

5 recordsLinked to original sources

PubMed1998

Identification of carbonic anhydrase activity in bullfrog olfactory receptor neurons: histochemical localization and role in CO2 chemoreception.

The objectives of this study were to determine: (1) the frequency and distribution of carbonic anhydrase (CA) activity in the bullfrog nasal cavities, and (2) whether inhibition of nasal CA affects the olfactory receptor response to CO2 or other odorants. It was found, using Hansson's staining technique, that some olfactory receptor neurons exhibited CA activity and that these CA-positive receptors were distributed throughout the nasal cavity with peak densities in the dorsal and ventral sensory epithelial regions. To test for the role of CA in olfactory transduction, electro-olfacto-grams (EOGs) were recorded from the surface of the ventral sensory epithelium in response to 2-s pulses of 5% CO2 and amyl acetate before and after topical CA inhibition with acetazolamide (10(-3) mol.l-1). In 52 bullfrogs, 1222 sites on the ventral epithelium were tested resulting in 23 locations that exhibited a response to 5% CO2. Inhibition of CA caused an immediate 65% reduction in the EOG response to CO2 while the response to amyl acetate was not affected. These results, along with the histochemical localization of CA in some olfactory receptor neurons, indicate that CA plays a role in the detection of CO2 in frog olfactory neurons and that only a small population of olfactory receptor neurons are CO2 sensitive.

Acetazolamide↗

PubMed1994

Measurements of the electron dose distribution near inhomogeneities using a plastic scintillation detector.

PURPOSE: Accurate measurement of the electron dose distribution near an inhomogeneity is difficult with traditional dosimeters which themselves perturb the electron field. We tested the performance of a new high resolution, water-equivalent plastic scintillation detector which has ideal properties for this application. METHODS AND MATERIALS: A plastic scintillation detector with a 1 mm diameter, 3 mm long cylindrical sensitive volume was used to measure the dose distributions behind standard benchmark inhomogeneities in water phantoms. The plastic scintillator material is more water equivalent than polystyrene in terms of its mass collision stopping power and mass scattering power. Measurements were performed for beams of electrons having initial energies of 6 and 18 MeV at depths from 0.2-4.2 cm behind the inhomogeneities. RESULTS: The detector reveals hot and cold spots behind heterogeneities at resolutions equivalent to typical film digitizer spot sizes. Plots of the dose distributions behind air, aluminum, lead, and formulations for cortical and inner bone-equivalent materials are presented. CONCLUSION: The plastic scintillation detector is suited for measuring the electron dose distribution near an inhomogeneity.

Electrodes↗

PubMed1994

Aggregation pathway of recombinant human keratinocyte growth factor and its stabilization.

Recombinant human keratinocyte growth factor (rhKGF) is prone to aggregation at elevated temperatures. Its aggregation pathway is proposed to proceed initially with a conformational change which perhaps results from repulsion between positively charged residues in clusters forming heparin binding sites. Unfolding of the protein leads to formation of large soluble aggregates. These soluble aggregates then form disulfide cross-linked precipitates. Finally these precipitates are converted to scrambled disulfides and/or non-disulfide cross-linked precipitates. Stabilizers such as heparin, sulfated polysaccharides, anionic polymers and citrate can greatly decrease the rate of aggregation of rhKGF at elevated temperatures. These molecules may all act by reducing charge repulsion on the protein thus stabilizing the native conformation. EDTA, on the other hand, is found to inhibit disulfide formation in aggregates and has only a moderate stabilizing effect on rhKGF.

Anions↗

PubMed1993

The self-efficacy-performance link in maximum strength performance.

To examine whether manipulating self-efficacy affects strength performance on a bench press, and to see if these situation-specific changes would affect levels of physical self-efficacy, 24 undergraduates untrained in weightlifting were randomly assigned to three groups: 'light', who lifted less weight than they believed; 'heavy', who lifted more weight than they believed; and control, for whom there was no manipulation. Self-efficacy measures were taken before and after the manipulation. Physical self-efficacy was measured using the Physical Self-Efficacy Scale (PSE). 'Light' subjects lifted significantly greater increases in weight than the other subjects. 'Heavy' subjects significantly decreased self-efficacy following the manipulation. Initial self-efficacy was found to be a significant predictor of baseline maximum, while manipulated self-efficacy was significant for performance change. The PSE scores did not change pre- to post-study. The results suggest that self-efficacy is a situation-specific construct which can be manipulated, and which relates to both past performance experience and future performance.

Adult↗

PubMed1992

Thrombin is a Na(+)-activated enzyme.

The amidase activity of human alpha-thrombin has been studied at steady state as a function of the concentration of several chloride salts, at a constant ionic strength I = 0.2 M. All kinetic steps of the catalytic mechanism of the enzyme have been solved by studies conducted as a function of relative viscosity of the solution. Among all monovalent cations, Na+ is the most effective in activating thrombin catalysis. This effect is observed with different amide substrates and also with gamma-thrombin, a proteolytic derivative of the native enzyme which has little clotting activity but retains amidase activity toward small synthetic substrates. The specific effects observed as a function of Na+ concentration are indicative of a binding interaction of this monovalent cation with the enzyme. The basis of this interaction has been explored by measurements of substrate hydrolysis collected in a three-dimensional matrix of substrate concentration, relative viscosity, and Na+ concentration, keeping the ionic strength constant with an inert cation such as choline or tetraethylammonium. The data have globally been analyzed in terms of a kinetic linkage scheme where Na+ plays the role of an allosteric effector. The properties of the enzyme change drastically upon binding of Na+, with substrate binding and dissociation, as well as deacylation, occurring on a time scale which is 1 order of magnitude faster. The apparent association constants for Na+ binding to the various intermediate forms of the enzyme have all been resolved from analysis of experimental data and are in the range of 50-100 M-1 at 25 degrees C. Studies conducted at different temperatures, in the range 15-35 degrees C, have revealed the enthalpic and entropic components of Na+ binding to the enzyme. The results obtained from steady-state measurements are supported by independent measurements of the intrinsic fluorescence of the enzyme as a function of Na+ concentration at a constant ionic strength I = 0.2 M, over the temperature range 15-35 degrees C. These measurements are indicative of a drastic conformational change of the enzyme upon Na+ binding to a single site. The energetics of Na+ binding derived from analysis of fluorescence measurements agree very well with those derived independently from steady-state determinations. It is proposed that thrombin exists in two conformations, slow and fast, and that the slow-->fast transition is triggered by binding of a monovalent cation. The high specificity in thrombin activation found in the case of Na+ is the result of its higher affinity compared to all other monovalent cations.(ABSTRACT TRUNCATED AT 400 WORDS)

Cations, Monovalent↗