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Biomedical subjects

B Partridge

Publications and source records attributed to B Partridge.

9 recordsLinked to original sources
PubMed1995

Ergosteroids: induction of thermogenic enzymes in liver of rats treated with steroids derived from dehydroepiandrosterone.

Dehydroepiandrosterone (DHEA), an intermediate in the biosynthesis of testosterone and estrogens, exerts several physiological effects not involving the sex hormones. When fed to rats it induces the thermogenic enzymes mitochondrial sn-glycerol-3-phosphate dehydrogenase and cytosolic malic enzyme in their livers. Animals and humans, and their excised tissues, are known to hydroxylate DHEA at several positions and to interconvert 7 alpha-hydroxy-DHEA, 7 beta-hydroxy-DHEA, 7-oxo-DHEA, and the corresponding derivatives of androst-5-enediol. We report here that these 7-oxygenated derivatives are active inducers of these thermogenic enzymes in rats and that the 7-oxo derivatives are more active than the parent steroids. We postulate that the 7 alpha-hydroxy and 7-oxo derivatives are on a metabolic pathway from DHEA to more active steroid hormones. These 7-oxo steroids have potential as therapeutic agents because of their increased activity and because they are not convertible to either testosterone or estrogens.

Animals↗
PubMed1994

Ulnar peripheral nerve stimulation by train-of-four technique in adult nonmedicated patients.

BACKGROUND: Peripheral nerve stimulation is necessary to quantify the level of neuromuscular blockade and prevent prolonged paralysis related to drug accumulation. Some nurses and physicians are hesitant to administer nerve stimulation because of concerns about inflicting pain on the patient. OBJECTIVE: To describe the feeling associated with train-of-four ulnar nerve stimulation, and to quantify discomfort, monitor heart rate response, and define the amount of current necessary to stimulate thumb adduction. METHODS: Healthy, nonmedicated volunteer subjects (N = 39) were asked to describe train-of-four ulnar nerve monitoring at 3 current strengths. Heart rate was monitored throughout the testing procedure. The milliamperes delivered at each current strength and the occurrence of thumb adduction were recorded. RESULTS: Subjects described nerve stimulation generally as an unusual prickly sensation. On a discomfort scale of 1 to 10, the mean discomfort score when stimulated with the current setting at 4 (15.5-23.6 mA) was 3.63. Level 4 stimulation produced thumb adduction in 54% of subjects. No heart rate change occurred in response to nerve stimulation. CONCLUSION: Nerve stimulation by train-of-four method was moderately uncomfortable but not painful. Heart rate response could not be relied on as a measurement of discomfort. Protocols for stimulation should include testing at level 4 and increasing as necessary to cause thumb adduction.

Adult↗
PubMed1981

An effective electron donor to cytochrome oxidase. Purification, identification, and kinetic characterization of a contaminant of ruthenium red, hexaamineruthenium II/III.

When the calcium-transport inhibitor, ruthenium red, is chromatographed on a cation exchange resin, it yields a number of colored fractions and a colorless component that absorbs in the ultraviolet. The electron transfer activity previously ascribed to ruthenium red (Schwerzmann, K., Gazzotti, P., and Carafoli, E. (1976) Biochem. Biophys. Res. Commun. 69, 812) fractionates exclusively with the UV-absorbing material. On the basis of spectral, physical, and activity studies, we have identified this compound as Ru(NH3)62+/3+. It is shown that Ru(NH3)62+/3+ is an efficient electron donor directly to cytochrome oxidase, without mediation by cytochrome c. The steady state kinetics of electron transfer from Ru(NH3)62+ to purified oxidase resembles that of cytochrome c, showing a biphasic pattern but higher apparent Km values (Km1 = 8 microM, Km2 = 88 microM). Under conditions that favor tight binding to the oxidase, cytochrome c acts as a competitive inhibitor of Ru(NH3)62+, indicating that the two electron donors interact with cytochrome oxidase at the same site(s). The efficiency of Ru(NH3)62+ as an electron mediator to cytochrome aa3 and the similarity of its kinetic behavior to that of cytochrome c, make it a potentially valuable tool for investigating the mechanism of energy conservation in the terminal segment of the mitochondrial respiratory chain.

Animals↗