ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Your email was sent successfully. Check your inbox.

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

Proceed reservation?

Export
Filter
  • Animals  (1)
  • Chemistry  (1)
  • Pulmonary tuberculosis  (1)
  • BIOTECHNOLOGY
  • 1980-1984  (3)
  • 1970-1974
  • 1925-1929
  • 1880-1889
  • 1984  (3)
  • 1
    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
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 2
    ISSN: 1432-0827
    Keywords: 1α25(OH)2D ; Hypercalcemia ; Normocalcemia ; Pulmonary tuberculosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Available evidence indicates that hypercalcemia in pulmonary tuberculosis results from increases in circulating 1α,25-dihydroxyvitamin D [1α,25(OH)2D]. To further characterize vitamin D metabolism in this disorder, the effects of vitamin D, 100,000 units a day for 4 days, were compared in 25 normal subjects and 11 patients with active pulmonary tuberculosis who were normocalcemic and had not had hypercalcemia. Serum calcium, phosphorus, 25-hydroxyvitamin D (25-OHD) and 1α,25(OH)2D were measured. Whereas vitamin D increased mean serum 25-OHD from 20±2 (±SE) to 40±5 ng/ml (P〈0.001) and did not change mean serum 1α,25(OH)2D in the normals (33±2 vs. 31±2 pg/ml), it increased mean serum 25-OHD from 21±4 to 55±13 ng/ml (P〈0.05) and mean serum 1α,25(OH)2D from 28±2 to 35±3 pg/ml (P〈0.05) in the patients. Serum calcium was normal and remained within the normal range in all subjects and patients. The findings indicate that there is a modest but significant abnormality in the regulation of circulating 1α,25(OH)2D in normocalcemic patients with pulmonary tuberculosis. The results are similar to those previously reported by us in normocalcemic patients with sarcoidosis.
    Type of Medium: Electronic Resource
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 23 (1984), S. 1249-1259 
    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
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...