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  • 1
    Electronic Resource
    Electronic Resource
    Haemodynamic, metabolic, and lymphocyte beta2-adrenoceptor changes following chronic beta-adrenoceptor antagonism (1987)
    Springer
    European journal of clinical pharmacology 32 (1987), S. 237-243 
    Details
    ISSN: 1432-1041
    Keywords: beta-antagonists ; beta2-adrenoceptor ; selectivity ; intrinsic sympathomimetic activity ; adrenaline hypokalaemia ; vasidilatation ; receptor up-regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Medicine
    Notes: Summary We have examined the effects of 7 days treatment with beta adrenoceptor antagonists in 8 healthy volunteers in a placebo controlled, crossover study. We investigated three beta-adrenoceptor antagonists (atenolol, oxprenolol, and propranolol), which have differing profiles of selectivity and partial agonist properties (intrinsic sympathomimetic activity, ISA). We studied adrenaline-induced hypokalaemia, the vasodilator response to an infusion of adrenaline (0.06 µg·kg−1·min−1 for 90 min), and lymphocyte beta2-adrenoceptor number, determined by (-) [125I]-iodocyanopindolol binding, and measured these variables both before and after 7 days of treatment. The beta2-mediated depressor response to adrenaline infusion was abolished by propranolol and oxprenolol but persisted after atenolol. In contrast, the hypokalaemia induced by adrenaline was abolished by all three beta-blockers. Lymphocyte beta2-adrenoceptor number increased significantly following propranolol treatment, but not after oxprenolol for atenolol. We conclude that up-regulation of lymphocyte beta2-adrenoceptors is dependent on beta2-receptor blockade and is modified by ISA. The reversal of the hypokalaemic response by atenolol suggests that beta1 receptors may contribute to the former effect. Alternatively, since different populations of beta2-adrenoceptors differ in their susceptibility to antagonists there may also be differences in agonist coupling to beta2-responses between tissues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00607569
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  • 2
    Electronic Resource
    Electronic Resource
    Fast atom bombardment and collisional activation mass spectrometry of retinyl phosphate mannose synthesized by liver membranes (1985)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 12 (1985), S. 221-227 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Fast atom bombardment (FAB) and collisional activation dissociation (CAD) mass-analysed ion kinetic energy (MIKE) spectra have confirmed the structures of retinyl phosphate (Ret-P), retinyl phosphate mannose (Ret-P-Man) and guanosine 5′-diphospho-D-mannose (GDP-Man). Ret-P-Man was made in vitro while Ret-P and GDP-Man were chemically synthesized. Positive ion FAB mass spectrometry of Ret-P showed an observable short-lived spectrum with a mass ion at m/z 367 [M + H]+, and a major fragment ion at m/z 269 [M+H—H3PO4]+. Negative ion FAB mass spectrometry of Ret-P showed a strong stable spectrum with a parent ion at m/z 365 [M—H]-, a glycerol (G) adduct ion at m/z 457 [M—H+G]- and a dimer ion at m/z 731 [2M—H]-. GDP-Man showed an intense spectrum with parent ion at m/z 604 [M—H]- and cationized species at m/z 626 [M+Na-2H]- and 648 [M+2Na-3H]-. Negative ion FAB mass spectrometry of Ret-P-Man showed a parent ion at m/z 527 [M—H]- and a fragment ion at m/z 259 [C6H12PO9]-. The CAD-MIKE spectra showed structurally significant fragment ions at m/z 442 and 361 for the [M—H]- ion of GDP-Man, and at m/z 509, 406, 364 and 241 for the [M—H]- ion of Ret-P-Man. FAB and CAD-MIKE spectra have been applied successfully to confirm the structure of Ret-P-Man made in vitro from Ret-P and GDP-Man.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200120507
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  • 3
    Electronic Resource
    Electronic Resource
    A novel hollow-fiber reactor with reversible immobilization of lactase (1988)
    Hoboken, NJ : Wiley-Blackwell
    AIChE Journal 34 (1988), S. 293-304 
    Details
    ISSN: 0001-1541
    Keywords: Chemistry ; Chemical Engineering
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Experimental and theoretical studies on a backflush hollow-fiber enzymatic reactor (HFER) were conducted in this work for a lactose/lactase system. An A. niger lactase was chosen, from the four lactases tested, for reversible immobilization in the sponge layers of the fibers. An enzyme loading procedure was developed that allowed reliable and reproducible operation of the hollow-fiber reactor and produced industrially significant conversions without apparent change in the activity or stability of the lactase used. This reversible immobilization scheme also permitted easy replacement of the enzyme used. The performance of the backflush HFER was investigated and a large number of data concerning its operation were obtained and interpreted. Momentum and mass transports in such a HFER were analyzed, and mathematical models that took the experimental findings into consideration were also developed and solved analytically and/or numerically. Predictions from the computer model developed in this work were found to be in excellent agreement with the experimental data collected, suggesting the possibility of a priori design of a process-scale backflush HFER. With minor modifications, the models developed are expected to be applicable to hollow-fiber reactors with a wide selection of immobilized cells, organelles, and other enzymes.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/aic.690340213
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