Dip-slide diagnosis of urinary-tract infection.
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Biomedical subjects
Publications and source records attributed to R H Davis.
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A survey of rhodanese activity (thiosulphate: cyanide sulphur transferase) in the tissues of the domestic fowl revealed that the highest activity occurred in the kidney, approximately twice that in the liver, 316 and 141 mumol SCN formed/min g protein, respectively. 2. In sparrows, pigeons and ducks, liver and kidney activities tended to be similar and increased with body size. 3. Relationships were found between enzyme activity and body weight to a fractional power, indicating relatively higher activity in smaller birds.
The response of Neurospora to changes in the availibility of exogenous arginine was investigated. Upon addition of arginine to the growth medium, catabolism is initiated within minutes. This occurs prior to expansion of the arginine pool or augmentation of catabolic enzyme levels. (Basal levels are approximately 25% of those found during growth in arginine-supplemented medium.) Catabolism of arginine is independent of protein synthesis, indicating that the catabolic enzymes are active but that arginine is not available for catabolism unless present in the medium. Upon exhaustion of the supply of exogenous arginine, catabolism ceases abruptly, despite an expanded arginine pool and induced levels of the catabolic enzymes. The arginine pool supports protein synthesis until the cells regain their normal capacity for endogenous arginine synthesis. These observations, combined with the known small level of induction of arginine catabolic enzymes, non-repressibility of most biosynthetic enzymes, and vesicular localization of the bulk of the arginine pool, suggest that compartmentation plays a significant role in controlling arginine metabolism in Neurospora.
During growth on minimal medium, cells of Neurospora contain three pools of ornithine. Over 95% of the ornithine is in a metabolically inactive pool in vesicles, about 1% is in the cytosol, and about 3% is in the mitochondria. By using a ureaseless strain, we measured the rapid flux of ornithine across the membrane boundaries of these pools. High levels of ornithine and the catabolic enzyme ornithine aminotransferase coexist during growth on minimal medium but, due to the compartmentation of the ornithine, only 11% was catabolized. Most of the ornithine was used for the synthesis of arginine. Upon the addition of arginine to the medium, ornithine was produced catabolically via the enzyme arginasn early enzyme of ornithine synthesis. The biosynthesis of arginine itself, from ornithine and carbamyl phosphate, was halted after about three generations of growth on arginine via the repression of carbamyl phosphate synthetase A. The catabolism of arginine produced ornithine at a greater rate than it had been produced biosynthetically, but this ornithine was not stored; rather it was catabolized in turn to yield intermediates of the proline pathway. Thus, compartmentation, feedback inhibition, and genetic repression all play a role to minimize the simultaneous operation of anabolic and catabolic pathways for ornithine and arginine.
We measured the metabolism of ornithine in Neurospora during the transition from minimal medium to arginine-supplemented medium. Within an hour after arginine supplementation, the amount of intracellular ornithine (95% of which had been stored in vesicles) dropped by 65%, even though the catabolism of arginine produces as much ornithine as had been produced on minimal medium. The arginine level in the cell rose 10-fold. Ornithine flux through the catabolic enzyme ornithine aminotransferase increased fivefold, but flux through the mitochondrial enzyme ornithine transcarbamylase (leading to arginine synthesis) was only 20% of the rate seen on minimal medium. During this transition to arginine catabolism, the enzymes of the arginine pathway operate as an ornithine cycle, but at a restricted rate. We suggest the hypothesis that high levels of arginine may inhibit the movement of ornithine into the vesicles and into the mitochondria.
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Spectrophotometric and thin-layer chromatographic methods for determination of imidocarb in biological specimens are described. Following intravenous injection of imidocarb (2.0 mg/kg) into 3 sheep, plasma concentrations, initially averaging 10.8 microgram/ml, decreased to an average of 1.9 microgram/ml within 1 hour and then to less than 1 microgram/ml within the next 4 hours. When imidocarb (4.5 mg/kg) was injected intramuscularly (IM) into 7 sheep, peak plasma concentrations averaging 7.9 microgram/ml were achieved within 4 hours and then rapidly decreased to 4.6 microgram/ml within the next 2 hours. Plasma values then decayed very slowly by first-order kinetics and trace amounts were still present 4 weeks after treatment. Imidocarb was bound to plasma proteins and the apparent volume of distribution was estimated to be slightly higher than the total body water. The concentrations of the drug in the plasma and in the erythrocytes were approximately equal. Detectable amounts were present in all examined tissues 4 weeks after IM administration Twenty-four hours after IM administration, the highest concentrations were in kidney, liver, and brain. The 14C-labeled imidocarb could be detected in all regions of the central nervous system examined, in the hypophysis, and in the pineal body. Metabolic or biotransformation products were not detected by the methods used. Of the administered IM dose, 11 to 17% was excreted in the urine within 24 hours; thereafter, the excretion rate was low, and detectable amounts were still present in the urine for 4 weeks. Renal clearance of imidocarb was less than glomerular filtration rate, indicating net tubular reabsorption. The relatively high concentration of imidocarb in the bile suggests that the bile is an important route of excretion. High concentrations were also found in the mild of lactating ewes, but the drug could not be detected in the plasma of lambs fed milk from these ewes.
In Neurospora cells grown on minimal medium, most of the large ornithine pool is found in osmotically sensitive organelles, the "vesicles." In this paper kinetic studies on the compartmental behavior of ornithine and its derivatives are reported. Analysis of the metabolism of a 10(-7) M pulse of uniformly labeled L-[14C] ornithine supports the following conclusions: (a) Over 98% of the cellular ornithine is in the vesicles. (b) The amount of ornithine normally in the cytosol is about 0.3% of the cellular ornithine, as shown by the kinetics of incorporation of 14C into putrescine via the cytosolic enzyme, ornithine decarboxylase (EC 4.1.1.17). (c) Mitochondria, the site of ornithine synthesis, contain about 1% of the cellular ornithine, as demonstrated by the kinetics of incorporation of 14C into citrulline via the mitochondrial enzyme, ornithine transcarbamylase (EC 2.1.3.3). (d) Considerable ornithine exchange, and a net efflux of ornithine, takes place across the mitochondrial membrane. (e) Ornithine aminotransferase (EC 2.6.1.13), a catabolic enzyme, may have a special relation to the cell membrane in cells grown in minimal medium. This enzyme uses ornithine efficiently while it enters from the medium, but very poorly after all the [14C] ornithine is within the cell. (f) Citrulline and proline are not compartmented with respect to the enzymes using them. (g) In contrast, arginine is distributed such that over 99% is in vesicles. We suggest that the vesicles; with their ability to sequester ornithine and arginine, are potentially significant in regulation.
Cytologic aspiration specimens of peritoneal fluid revealed that mesothelial cell proportions were significantly reduced 19.2% in women between 26 and 35 years of age. Possibly, mesothelial cell renewal was decreased in women of the older age groups.
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Senior staff of the departments of medicine, surgery and general practice in each medical school in the United Kingdom were asked to annotate the same case studies which had been prepared by medical students. Analysis of the annotations showed that general practitioners demanded much greater consideration by the student of the patient, his family and his environment, whereas physicians and surgeons tended to be more disease orientated. Nevertheless, expectations and attitudes of teachers in similar departments are remarkably diverse and this highlighted the potential role of the case study as an educational tool for staff and students alike. Many departments need to clarify the difference between undergraduate and postgraduate teaching objectives.
Since the cellular composition of peritoneal fluid is altered by sex, species, pregnancy, ovulation and the estrous as well as menstrual cycles we believe that the cellular content of peritoneal fluid is affected in a characteristic manner by the administration of hormones. Estrogen, progesterone, testosterone, chorionic gonadotropin, cortisone as well as various physiologic model situations were considered.
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Anesthetized adult female rhesus monkeys were impacted in the middle of the sternum with a 10 kg stunner traveling at a speed of 22-25 mph to simulate an automobile accident. Blodd was obtained at 10 and 60 min following the impact, and approximately 50 values were measured with an autoanalyzer. Blunt chest shock and trauma produced a biochemical, hematologic, and urinary profile which might be used to aid life saving measures.
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