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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Pharmaceutical research 17 (2000), S. 38-41 
    ISSN: 1573-904X
    Keywords: absorption ; aerosols ; surface active agents ; drug administration routes ; drug formulation ; radioactive imaging
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Purpose. Small solutes which are deposited in the alveoli by aerosolinhalation will be absorbed across the alveolo-capillary barrier.Inhalation of dioctyl sodium sulfosuccinate (DOSS) enhances absorptionwhile having little or no effect on lung function, suggesting that surfaceactive agents may be used as enhancers of alveolar absorption ofinhaled pharmaceuticals. The purpose of this study was to examinethe effects of a selection of different surface active agents onalveolar absorption. Methods. The absorption of 99mTc-diethylene triamine pentaacetate(99mTc-DTPA) from the lungs was studied in rabbits. We studied fivedifferent surface active agents: DOSS, sodium glycodioxycholate(GDCA), sodium lauryl sulphate (NaLS), lysophosphatidyl choline(LPC) and polyoxyethylene-23-laurylether (P23LE). Results. DOSS and GDCA both dramatically enhanced the absorptionof 99mTc-DTPA. There was a moderate effect of NaLS, no significanteffect of LPC and P23LE reduced the rate of absorption. None of thecompounds affected gas exchange or lung compliance. Conclusions. There is a wide spectrum of effects of inhaled surfaceactive agents on the alveolar absorption of 99mTc-DTPA. Ioniccompounds such as DOSS and GDCA have the greatest effect, and furtherstudies of these classes of surface active agents for use as enhancersof alveolar absorption of pharmaceuticals seem warranted.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4943
    Keywords: Alkaline phosphatase ; inhibition ; chemical modification ; N-bromosuccinimide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The inactivation of alkaline phosphatase from green crab (Scylla serrata) by N-bromosuccinimide has been studied using the kinetic method of the substrate reaction during modification of enzyme activity previously described by Tsou [(1988),Adv. Enzymol. Related Areas Mol. Biol. 61, 381–436]. The results show that inactivation of the enzyme is a slow, reversible reaction. The microscopic rate constants for the reaction of the inactivator with free enzyme and the enzyme-substrate complex were determined. Comparison of these rate constants indicates that the presence of substrate offers marked protection of this enzyme against inactivation by N-bromosuccinimide. The above results suggest that the tryptophan residue is essential for activity and is situated at the active site of the enzyme.
    Type of Medium: Electronic Resource
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