Ethics in theory and practice. Let's be practical.
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Biomedical subjects
Publications and source records attributed to H O Thompson.
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A prospective study was begun using ultrasound to diagnose defects in the lower uterine segment. Seventy patients were examined and delivered by cesarean section, including 58 at risk because of previous cesarean section and 12 nulliparous controls not at risk. Of the at-risk patients, 12 had confirmed defects, for an incidence of 20.7%. All the controls were normal. The false-positive rate for at-risk patients was 7.1%, and the positive and negative predictive values were 92.3 and 100%, respectively. For the diagnosed cases, the sonographic lower uterine segment seemed to form earlier (P less than .01) and was thinner (P less than .01) than that in the negative cases or the controls. Although our study design was observational and did not allow us to test the performance of the lower uterine segment when a defect was found, we discuss the use of a three-stage classification system to assist in identifying sonographically detected defects in a future trial of labor protocol. We conclude that sonographic surveillance is a reliable and practical means of evaluating the lower uterine segment after conception and before labor or delivery.
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The reactions of penicillamine with gold sodium thiomalate (Myochrysine), gold-albumin complexes, and gold bound to urinary and kidney cytosolic proteins were examined. Large excesses of penicillamine (20 to 100:1 penicillamine/gold ratios) are required to mobilize significant amounts of protein bound gold. Quantitative comparisons of cysteine and penicillamine displacements of serum albumin bound gold indicate that penicillamine is approximately 5-6 times more effective than cysteine. Urinary gold is observed to be present in low molecular weight and protein bound forms, which exist in a labile chemical equilibrium and can be shifted by addition of penicillamine. These results are discussed in terms of the structure of gold(I)-penicillamine complexes and the distribution of gold(I) among protein and nonprotein thiol groups. The inappropriateness of using AuCl4- in vitro to study the biochemistry of chrysotherapy agents is delineated.
L-Cysteinatogold(I) was prepared by the reaction of L-cysteine with KAuBr4 in acidic media and its solubility determined from pH 4 to 10. The solubility at pH 7.4 and 37 degrees C is 1 microM. In the presence of excess cysteine, the solubility increases because of formation of bis(L-cysteinato)gold(I). The equilibrium-constant for formation of the bis complex is 2.1 +/- 0.4 X 10(-3), which at pH 7.4 CORRESPONDs to an apparant formation constant of 4.4 X10(4). The formation of the bis adduct was confirmed by chromatographic separation of the products of the reaction between [35S]-L-cysteine and Na2AuTM. This complex elutes with Kav = 1.15 which allows it to be distinguished from other gold thiolates that might form in vivo. The bis(cysteinato)gold(I) complex is shown to be present in kidney cytosol isolated from rats given Na2AuTM in vivo. When additional cysteine is added to the cytosol in vitro, the peak at 1.15 is increased, but if glutathione is added, the low molecular weight gold elutes at Kav = 1.00, which is taken as evidence for the existence of bis(cysteinato)gold(I) in the cytosol preparation. The amount of gold present as bis(cysteinato)gold(I) after 4 different dose schedules has been measured and found to increase with the total cytosol gold concentration. L-Cysteinatogold(I) does not dissolve in the presence of bovine serum albumin to form an adduct.
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