J. G. Spenney

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Gel filtration and anion-exchange chromatography have been used to investigate whether 3'-phosphoadenylylsulfate:bile salt sulfotransferase activity from female rat and hamster liver is heterogeneous. Using these techniques at least three different enzyme activities were demonstrated with two different bile salt substrates. In both animals, but particularly(More)
1. A simplified technique for the measurement of bile-acid pool size and synthesis rate has been developed in patients with liver disease. Isotope dilution studies in blood and bile were performed after intravenous injection of [24-14C]cholic acid with radioimmunoassay for the measurement of the bile-acid concentration. The interpolated pool sizes and(More)
The NADH oxidoreductase reaction with resazurin was most rapid at pH 6.5. FMN (10 mumol/l) markedly stimulated the reaction, and the optimal concentration of resazurin was 50 mumol/l. The oxidation of NADH by NADH oxidoreductase with resaruzin as electron acceptor gave a variable yield of fluorescent product, resorufin. The yield was pH dependent and was(More)
Knowledge of the biochemical basis of gastric acid secretion has progressed dramatically in the last 25-30 years. Today, only the overall physiological consequences can be described by the carbonic anhydrase reaction; the biochemical details are much more complicated and remain incompletely resolved. The controversy between a redox, directly substrate(More)
The evolutionary homology of pepsinogens was further evaluated by isolating and characterizing the pepsinogen of the esophageal glands of Rana catesbeiana. Like other pepsinogens, this esophageal enzyme was activated by acid; the resulting pepsin was optimally active between pH 1.4 and 2.0, and was irreversibly denatured above pH 7.0. Chromatography on(More)
The mechanisn of hydrolysis of acetylsalicylate during absorption from the gastrointestinl tract has been investigated by identification, quantitation, and purification of a hydrolase from gastric mucosal homogenates. The hydrolase was found to be a soluble, cytosolic enzyme with a pH optimum in the slightly alkaline range, pH 8.6 Acetylsalicylate hydrolase(More)