ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    facet.materialart.
    Unknown
    Polyene toxicity in renal medulla: injury mediated by transport activity (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-04-06
    Description: Polyene antibiotics such as amphotericin and nystatin increase membrane permeability and thus increase the amount of oxygen consumed in active electrolyte transport. In isolated perfused rat kidneys, the polyenes produced extensive injury to the medullary thick ascending limb, a segment of the nephron with limited oxygen supply. This damage was prevented if reabsorptive transport was inhibited by ouabain. Cell death under these circumstances thus appears to be mediated by increased oxygen demand for transport activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brezis, M -- Rosen, S -- Silva, P -- Spokes, K -- Epstein, F H -- AM18078/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1984 Apr 6;224(4644):66-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6322305" target="_blank"〉PubMed〈/a〉
    Keywords: Amphotericin B/adverse effects ; Animals ; Biological Transport, Active/drug effects ; Cell Membrane Permeability/drug effects ; Furosemide/pharmacology ; Glomerular Filtration Rate/drug effects ; Kidney Medulla/*drug effects/pathology ; Loop of Henle/drug effects ; Nystatin/adverse effects ; Ouabain/pharmacology ; Oxygen Consumption/drug effects ; Polyenes/*adverse effects ; Rats ; Sodium/metabolism ; Sodium-Potassium-Exchanging ATPase/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 2
    Electronic Resource
    Electronic Resource
    Kinetics of irreversible dissociation for proteins bound cooperatively to DNA (1984)
    New York : Wiley-Blackwell
    Biopolymers 23 (1984), S. 1249-1259 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: We consider the irreversible dissociation kinetics of proteins that bind cooperatively and nonspecifically to DNA. Our model consists of an infinitely long one-dimensional nucleic acid lattice on which are bound protein ligands. A set of adjacent bound proteins forms a cluster of length n. A protein molecule may dissociate from any site within the bound cluster, not only from the ends, as was assumed in a previous model of this process due to Lohman [(1983) Biopolymers 22, 1697-1713]. By considering this additional pathway, we present a more general treatment of the dissociation kinetics of cooperatively bound ligands. We show that dissociation from the (n-2) internal positions of an n-cluster is an important pathway when the initial fractional saturation of the lattice is close to unity and the co operatively is low. When the fractional saturation is initially equal to 1 and the co operatively is low, our model does not give the zero-order dissociation kinetics predicted by the Lohman model.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360230709
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...