Studies on Kallikreins. VI. Effect of pancreatic kallikrein and kinin on the transport of amino acids and glucose across the rat small intestine.
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Biomedical subjects
Publications and source records attributed to H Fujimori.
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The flow of glucose and valine from the mucosal to the serosal side of rat intestine was stimulated significantly by kallikrein-kinin system. To elucidate the mechanism of this function the effects of kallidin on the transmural potential difference (PDt) between the serodal and the mucosal sides and the transepithelial resistance (Rt) of rat jejunum segment were investigated by electrophysiological procedures. The glucose-evoked PDt was not significantly altered by addition of kallidin to the mucosal fluid. Meanwhile, PDt which evoked by glucose was significantly shifted under the presence of 10-1-10(2) ng kallidin in the serosal fluid. The valine-evoked PDt was also changed by addition of 10 ng kallidin into the serosal fluid. However, the addition of glucose to the mucosal and kallidin to the serosal fluid did not affect on the Rt of the jejunum segment. These results suggest that kinin stimulated Na+ transport at the baso-lateral membrane of the intestinal absorptive cells, and the transports of other substances were enhanced consequently.
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A series of 6-phenyl-4H-pyrrolo[1,2-a][1,4]benzodiazepines (2) has been prepared with 2-phthalimidomethylfurans (12) and 1-phthalimidoalkane-2,5-diones (15) or 2,5-dimethoxy-2-phthalimidomethyltetrahydrofurans (16) as the key intermediates and subsequently evaluated for CNS activity. The structure-activity data generated indicate that, in general, introduction of the methyl and/or ethyl group(s) in the pyrrole ring and a chlorine atom at the ortho position of the 6-phenyl group increases the activity and that substitution of the above chlorine atom for a fluorine atom decreases the activity. 8-Chloro-6-(2-chlorophenyl)-1,3-dimethyl-4H-pyrrolo[,2-a][1,4]benzodiazepine (2p), the most potent among the compounds synthesized, was equipotent in taming and sedative activities to diazepam. The acute LD50 of 2p in mice was larger than 3000 mg/kg po.
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Four tryptophan residues of saccharifying alpha-amylase from B. subtilis out of eleven in total are reactive towards N-bromosuccinimide (NBS), suggesting that they are on the surface of the enzyme. This is consistent with the results of solvent perturbation difference spectrophotometry with ethylene glycol. One of four tryptophan residues was clearly distinguished from the other three in reactivity with NBS by the stopped-flow method. This most reactive tryptophan residue was not protected from modification by substrates of analogs, indicating that the tryptophan is not located in the substrate binding site. One of the other three tryptophan residues, probably the second most reactive one, is considered to be related in some way to the glycosyl transfer in the reaction of the enzyme with maltose as a substrate.
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