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  • General Chemistry  (1)
  • bronchi  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Chemistry - A European Journal 2 (1996), S. 759-766 
    ISSN: 0947-6539
    Keywords: ionophores ; impedance spectroscopy ; membrane models ; monolayers ; self-assembly ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Novel ion-binding monolayers on gold surfaces are presented where the molecular design is based upon the natural ion binder ferrichrome. The new ion binders possess hydroxamate coordinating groups arranged in C2 symmetry (bishydroxamate binder, BHB) or C3 symmetry (trishydroxamate binder, THB), and a separate dialkyl sulfide moiety, which serves as an anchor to the gold substrate. The separation between the ion-binding cavity and the attachment site to the gold allows each parameter to be controlled separately, namely, cavity size, its symmetry and external envelope, as well as the functional group used for immobilization. The monolayers were characterized with respect to ellipsometric thickness, wettability (advancing and receding contact angles (CAs) for water), and surface coverage; the latter is determined by metal underpotential deposition (UPD). It is shown that the introduction of hydrophobic side chains (i-butyl) improves the CAs, thickness, and surface coverage of the monolayers. A detailed analysis of the alternating-current (AC) impedance spectra is presented for THB monolayers on gold electrodes, where the impedance data are fitted to an equivalent circuit model. It is shown that the AC response in a wide frequency range can be used to probe ion binding and release in monolayer systems on electrodes.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 53 (1993), S. 352-359 
    ISSN: 0730-2312
    Keywords: airway ; bronchi ; peptidases ; proteinase inhibitors ; dexamethasone ; inflammation ; zinc ; chloride ; RU 38486 ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The purpose of this study was to determine whether angiotensin I-converting enzyme (ACE) is present in cultured bovine bronchial epithelial cells (BBECs) and whether its activity can be modulated. We found that extracts of confluent monolayers of cultured BBECs degraded [glycine-1-14C]hippuryl-L-histidyl-L-leucine at a rate of 843 ± 66 pmol/hr/mg protein (mean ± SEM, n = 5). In addition, we found that the enzyme was shed into the culture medium. ACE activity in BBECs was inhibited by three selective, but structurally different, ACE inhibitors (captopril, quinapril, and cisalaprilat) with an IC50 of approximately 2 nM. Increasing chloride concentration in the assay buffer resulted in an increase in BBECs ACE activity of 63%. Enzyme activity was also modulated by the presence of zinc cation in the assay buffer. Addition of dexamethasone to the culture medium was associated with a significant increase in BBECs ACE activity (P 〈 0.05), which was inhibited by the steroid receptor antagonist RU 38486. Western blot analysis of BBECs, tracheal and bronchial mucosal strips utilizing a cross-reacting rabbit anti-mouse ACE antibody, showed a faint 175 kDa band and additional strong 52 kDa and 47 kDa band. The mechanism of generation of the low M.W. bands is unknown. Our data indicate the presence of ACE in cultured BBECs and that enzyme activity can be modulated.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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