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  • 1
    ISSN: 1432-1912
    Keywords: Glucose transport ; IAPS-forskolin ; Insulin-regulated glucose transporter GLUT4
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Two arginine residues (RR333/334) in the conserved GRR motif located in the endofacial loop between helix 8 and 9 of the glucose transporter GLUT4 were substituted for leucine and alanine, respectively. Reconstituted glucose transport activity of the construct (GLUT4-RR333/4LA) expressed in COS-7 or LM(TK-) cells was less than 10% of that of the wild-type GLUT4. In contrast, binding of the inhibitory ligand cytochalasin B and glucose-inhibitable photolabeling with IAPS-forskolin were not significantly affected. Exchange of a histidine residue (H337Q) previously believed to be involved in the binding of inhibitory ligands failed to affect any of the investigated parameters. These data suggest that positive charges in the GRR motif at the cytoplasmic surface of the transporter participate in the conformational changes of the carrier protein during the process of facilitated diffusion.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-1912
    Keywords: Key words Glucose transport ; IAPS-forskolin ; Insulin-regulated glucose transporter GLUT4
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Two arginine residues (RR333/334) in the conserved GRR motif located in the endofacial loop between helix 8 and 9 of the glucose transporter GLUT4 were substituted for leucine and alanine, respectively. Reconstituted glucose transport activity of the construct (GLUT4-RR333/4LA) expressed in COS-7 or LM(TK–) cells was less than 10% of that of the wild-type GLUT4. In contrast, binding of the inhibitory ligand cytochalasin B and glucose-inhibitable photolabeling with IAPS-forskolin were not significantly affected. Exchange of a histidine residue (H337Q) previously believed to be involved in the binding of inhibitory ligands failed to affect any of the investigated parameters. These data suggest that positive charges in the GRR motif at the cytoplasmic surface of the transporter participate in the conformational changes of the carrier protein during the process of facilitated diffusion.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 13 (1967), S. 1155-1159 
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The pressure drop of water was measured when water flowed through a bed of stainless steel ball bearings packed in an ordered rhombohedral geometry. Experiments were carried out with eleven different packed beds, encompassing the entire range of the square-base array, in the same 10.85 by 10.85 by 30-in. rectangular test column in a forced circulation loop at modified Reynolds numbers up to 17,000. The test variables included water velocity, bed voidage, spacing between adjacent balls, ball diameter, and bed height. Curves of friction factor vs. Reynolds number are presented. An increase in the relative horizontal spacing between balls was found to have a more important effect than an increase in voidage in decreasing the pressure drop. A general correlation relating the mutual effects of bed voidage and ball spacing on pressure drop that would bring all the data points together, especially in the transition flow region, could not be found. As a result, the system appears to consist of two distinct parts separated at the minimum packing density. A correlation was found only for the first, but from a practical point of view more important, region. Data may be corrected for bed voidage, but only for small variations in ball spacing, by the ratios of (1 - ε)/ε3 at the two voidages. No entrance and exit effects could be measured beyond the first seven ball layers.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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