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  • 1
    Electronic Resource
    Electronic Resource
    Luminal dopamine modulates canine ileal water and electrolyte transport (1995)
    Springer
    Digestive diseases and sciences 40 (1995), S. 1738-1743 
    Details
    ISSN: 1573-2568
    Keywords: dopamine ; α-adrenergic ; intestinal transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Previous studies have suggested that dopamine stimulates active ileal ion absorption viaα 2-adrenergic or dopaminergic receptor activation. Identification of a dopamine 1a receptor on rat enterocytes located in intestinal crypts prompted this investigation of the effect of luminally administered dopamine on water and ion transport in the canine ileum. Absorption studies (n=27) were performed in dogs with 25-cm ileal Thiry-Vella fistulas. Perfusion with [14C PEG was used to calculate absorption of water and electrolytes from the Thiry-Vella fistula. Experiments consisted of three 1-hr periods: basal, luminal drug infusion at 10−4 M, and recovery. Agonists used included dopamine (DOP: α-adrenergic, D1 and D2 receptor) and SKF 38393 (D1 receptor). Antagonists used included terazosin (TZ:α 1) and yohimbine (YOH:α 2). DOP caused significant increases in water and electrolyte absorption. TZ and YOH prevented the dopamine-induced proabsorptive response. Luminal DOP may serve as a proabsorptive modulator of ileal transport, acting viaα 1,α 2, and dopaminergic receptors. The development of more potent proabsorptive dopamine analogs, which maintain the ability to broadly activate mucosal receptors, may be useful in such clinical situations as diabetic diarrhea, short gut syndrome, or following small bowel transplantation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02212695
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Production and purification of a fused recombinant protein gp-36 (HIV-2) from Escherichia coliThis paper was presented at the Third International Conference on Separations for Biotechnology, N. 66, 12-15 September 1994, Bulmershe Court, University of Reading, UK. (1996)
    Chichester : Wiley-Blackwell
    Journal of Chemical Technology AND Biotechnology 66 (1996), S. 1-6 
    Details
    ISSN: 0268-2575
    Keywords: recombinant fusion protein ; gp-36 HIV-2 ; inclusion bodies ; purification ; Escherichia coli ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: A fragment of the gp-36 gene of the Human Immunodeficiency Virus type 2 (HIV-2) was fused to a stabilizer sequence, which encodes for the first N-terminal 58 amino acids of the human interleukin-2. The fused protein was expressed under the control of the tryptophan promoter in Escherichia coli, and expressed as 20% of the total cellular protein. Transmission electron microscopy indicated that the fusion protein formed cytoplasmic insoluble inclusion bodies. Inclusion bodies were semipurified by a wash pellet cell procedure, rendering a material with a purity higher than 70% by SDS-polyacrylamide gel electrophoresis. After solubilization with urea, this preparation was further purified by gel-filtration chromatography up to 95% purity.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
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