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  • Animals  (137)
  • FLUID MECHANICS AND HEAT TRANSFER  (68)
  • 1980-1984  (205)
  • 1982  (205)
  • 1
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    Hyperglycemia of diabetic rats decreased by a glucagon receptor antagonist (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-02-26
    Description: The glucagon analog [l-N alpha-trinitrophenylhistidine, 12-homoarginine]-glucagon (THG) was examined for its ability to lower blood glucose concentrations in rats made diabetic with streptozotocin. In vitro, THG is a potent antagonist of glucagon activation of the hepatic adenylate cyclase assay system. Intravenous bolus injections of THG caused rapid decreases (20 to 35 percent) of short duration in blood glucose. Continuous infusion of low concentrations of the inhibitor led to larger sustained decreases in blood glucose (30 to 65 percent). These studies demonstrate that a glucagon receptor antagonist can substantially reduce blood glucose levels in diabetic animals without addition of exogenous insulin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, D G -- Goebel, C U -- Hruby, V J -- Bregman, M D -- Trivedi, D -- AM21085/AM/NIADDK NIH HHS/ -- AM25318/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1982 Feb 26;215(4536):1115-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6278587" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Diabetes Mellitus, Experimental/*drug therapy ; Glucagon/*analogs & derivatives/*antagonists & inhibitors/therapeutic use ; Hyperglycemia/*drug therapy ; Male ; Rats ; Receptors, Cell Surface/*drug effects ; Receptors, Glucagon ; Structure-Activity Relationship
    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)
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  • 2
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    Mean flowfields in axisymmetric combustor geometries with swirl (1982)
    In:  Other Sources
    Details
    Publication Date: 2019-07-13
    Description: Six flowfield configurations are investigated with sidewall angles of 90 and 45 deg, and swirl vane angles of 0, 45, and 70 deg. It is found that central recirculation zones occur for the swirling flow cases investigated, which extend from the inlet to x/D = 1.7, where x is the axial polar coordinate, and D is the test section diameter. Five-hole pitot probe pressure measurements are used to determine time-mean velocities, and corresponding flow situations are predicted and compared to results of experimental data. Excellent agreement is found for the nonswirling flow, although poor agreement is found for swirling flow cases, especially near the inlet. The discrepancy is attributed to the lack of realism in the turbulence model, and/or to inaccurate specification of time-mean velocity and turbulence energy distributions at the inlet.
    Keywords: FLUID MECHANICS AND HEAT TRANSFER
    Type: AIAA PAPER 82-0177 , Aerospace Sciences Meeting; Jan 11, 1982 - Jan 14, 1982; Orlando, FL
    Format: text
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    NASA TECHNICAL REPORTS
  • 3
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    Complete amino acid sequence of urotensin I, a hypotensive and corticotropin-releasing neuropeptide from Catostomus (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-10-08
    Description: Urotensin I, purified from extracts of the urophysis of a teleost fish (Catostomus commersoni), exhibits potent hypotensive activity (mammals and birds) and corticotropin-releasing activity (both fish and mammals). The primary structure of this 41-residue peptide was determined to be H-Asn-Asp-Asp-Pro-Pro-Ile-Ser-Ile-Asp-Leu-Thr-Phe-His-Leu-Leu-Arg-Asn-Met-Ile-Glu - Met-Ala-Arg-Ile-Glu-Asn-Glu-Arg-Glu-Gln-Ala-Gly-Leu-Asn-Arg-Lys-Tyr-Leu-Asp-Glu -Val-NH2. Extraction with 0.1N HCl at 100 degrees C cleaves the amino-terminal tripeptide, yeilding a fully active analog, urotensin I(4-41). The amino acid sequence was confirmed by measuring the biological activity of synthetic urotensin I(4-41). Urotensin I exhibits a striking sequence homology with ovine corticotropin-releasing factor and with frog sauvagine. These three peptides exhibit similar activities in biological test systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lederis, K -- Letter, A -- McMaster, D -- Moore, G -- Schlesinger, D -- New York, N.Y. -- Science. 1982 Oct 8;218(4568):162-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6981844" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Corticotropin-Releasing Hormone ; Fishes ; Peptides/*isolation & purification ; Species Specificity ; Urotensins/*isolation & purification
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Significance of tissue myo-inositol concentrations in metabolic regulation in nerve (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-08-27
    Description: Approximately 25 percent of resting energy utilization in isolated nerve endoneurium is inhibited by medium containing defatted albumin and selectively restored by arachidonic acid but is unaffected by indomethacin or nordihydroguaiaretic acid. The same component of energy utilization is inhibited by small decreases in endoneurial myo-inositol, which decrease incorporation of carbon-14-labeled arachidonic acid into phosphatidylinositol. The fraction of the resting oxygen uptake inhibited by ouabain is decreased 40 to 50 percent by a reduced tissue myo-inositol concentration or by defatted albumin. Metabolic regulation by rapid, basal phosphatidylinositol turnover is dependent on the maintenance of normal tissue myoinositol concentrations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simmons, D A -- Winegrad, A I -- Martin, D B -- T32 AMO7314/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1982 Aug 27;217(4562):848-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6285474" target="_blank"〉PubMed〈/a〉
    Keywords: Albumins/pharmacology ; Animals ; Arachidonic Acid ; Arachidonic Acids/pharmacology ; Catechols/pharmacology ; Indomethacin/pharmacology ; Inositol/*metabolism ; Linolenic Acids/pharmacology ; Masoprocol ; Ouabain/pharmacology ; Oxygen Consumption ; Palmitic Acids/pharmacology ; Peripheral Nerves/*metabolism ; Phosphatidylinositols/metabolism ; Rabbits ; gamma-Linolenic Acid
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Lethal effect of phenothiazine neuroleptics on the pathogenic protozoan Leishmania donovani (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-07-23
    Description: Phenothiazine drugs, which are widely used for their antipsychotic, antianxiety, and antiemetic effects, have been found to have protozoacidal effects on the human pathogen Leishmania donovani. These compounds are lethal to both the extracellular stage of the organism, which is inoculated into humans by the sand fly, and the intracellular stage, which is found solely in human macrophages during established infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pearson, R D -- Manian, A A -- Harcus, J L -- Hall, D -- Hewlett, E L -- New York, N.Y. -- Science. 1982 Jul 23;217(4557):369-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6124040" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antipsychotic Agents/*pharmacology/therapeutic use ; Chlorpromazine/pharmacology ; Cricetinae ; Humans ; Leishmania/*drug effects ; Leishmaniasis, Visceral/*drug therapy ; Macrophages/microbiology ; Mesocricetus
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Asian bull elephants: Flehmen-like responses to extractable components in female elephant estrous urine (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-07-09
    Description: Flehmen-like responses (urine tests) are one of the characteristic behavioral reactions of male Asian elephants (Elephants maximus) to cow elephants in estrus. Components of the urine of estrous cow elephants were extracted with organic solvents and partially purified by chromatography and shown to evoke Flehmen-like responses when they were presented to adult bulls.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rasmussen, L E -- Schmidt, M J -- Henneous, R -- Groves, D -- Daves, G D Jr -- New York, N.Y. -- Science. 1982 Jul 9;217(4555):159-62.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7089549" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Elephants/anatomy & histology/*physiology ; Estrus Detection ; Female ; Male ; Pheromones/*urine ; Sex Attractants/isolation & purification/*urine ; *Sexual Behavior, Animal
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Transmethylation of phosphatidylethanolamine: an initial event in embryonic chicken lens fiber cell differentiation (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-09-24
    Description: Agents that induce differentiation of lens epithelial cells into lens fiber cells in vitro transiently stimulate the transmethylation of phosphatidylethanolamine. Inhibition of transmethylation by 3-deazaadenosine results in a corresponding inhibition of the cell elongation that characterizes lens fiber formation, suggesting that phospholipid methylation plays an essential role in the differentiation of these cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zelenka, P S -- Beebe, D C -- Feagans, D E -- New York, N.Y. -- Science. 1982 Sep 24;217(4566):1265-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7112130" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation/drug effects ; Chick Embryo ; Lens, Crystalline/*cytology/metabolism ; Methylation ; Phosphatidylcholines/*biosynthesis ; Phosphatidylethanolamines/*metabolism ; Tubercidin/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Saxitoxin binding sites in frog-myocardial cytosol (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-02-26
    Description: Cytosolic fractions of frog heart homogenates contain large amounts of a soluble, large molecular weight protein that binds the specific neurotoxin saxitoxin with the same high affinity as does the plasma membrane. Another neurotoxin, tetrodotoxin, which ordinarily is competitive with saxitoxin, does not displace saxitoxin from the cytosolic sites or from plasma membrane-enriched vesicular fractions even when its concentration exceeds that of saxitoxin by a factor of 1000. Thus, cytosolic sites are similar to membrane sites in this respect. The vesicular fraction accounts quantitatively for the amount of saxitoxin bound by whole ventricles, so that no appreciable losses seem to occur. Therefore, the cytosolic site probably is a membrane site precursor, although other possibilities cannot be ruled out. In any case, the occurrence of a soluble molecule closely related to the sodium channel provides opportunities for further study of the structure of the sodium channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doyle, D D -- Wong, M -- Tanaka, J -- Barr, L -- New York, N.Y. -- Science. 1982 Feb 26;215(4536):1117-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6278588" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/metabolism ; Cytosol/metabolism ; Ion Channels/metabolism ; Myocardium/*metabolism ; Protein Binding ; Rana pipiens ; Saxitoxin/*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)
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  • 9
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    An estrogen-binding protein and endogenous ligand in Saccharomyces cerevisiae: possible hormone receptor system (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-10-15
    Description: A protein macromolecule in the cytosol of the unicellular eukaryotic yeast Saccharomyces cerevisiae selectively binds the vertebrate estrogen hormone 17 beta-estradiol with high affinity. Lipid extracts of the yeast cells or the conditioned growth medium yield a substance that can bind competitively to the tritiated estradiol-binding sites in the yeast and to mammalian estrogen receptors. These findings suggest that the binding protein may be a primitive hormone receptor and that the lipid-extractable substance represents the endogenous ligand.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feldman, D -- Do, Y -- Burshell, A -- Stathis, P -- Loose, D S -- GM28825/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1982 Oct 15;218(4569):297-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6289434" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding, Competitive ; Chromatography, High Pressure Liquid ; Cytosol/metabolism ; Female ; Ligands ; Rats ; Receptors, Cell Surface/metabolism ; Receptors, Estrogen/*analysis ; Saccharomyces cerevisiae/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Spinal sympathetic neurons: possible sites of opiate-withdrawal suppression by clonidine (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-03-26
    Description: Morphine, methadone, meperidine, fentanyl, and clonidine rapidly depressed transmission through sympathetic preganglionic neurons in cats with the spinal cord transected. Naloxone promptly antagonized this effect of the opiates but not that of clonidine which was reversed by alpha 2-adrenergic receptor antagonists. The independent depression of preganglionic neurons by clonidine may contribute to the ability of this drug to depress the symptoms of opiate withdrawal that are characterized by sympathetic hyperactivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Franz, D N -- Hare, D B -- McCloskey, K L -- GM-07579/GM/NIGMS NIH HHS/ -- HL-24085/HL/NHLBI NIH HHS/ -- RR-05428/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1982 Mar 26;215(4540):1643-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6280276" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cats ; Clonidine/*pharmacology/therapeutic use ; Evoked Potentials/drug effects ; Humans ; Narcotics/pharmacology ; Receptors, Drug/drug effects ; Reflex/drug effects ; Spinal Cord/cytology ; Structure-Activity Relationship ; Substance Withdrawal Syndrome/*drug therapy ; Sympathetic Nervous System/*drug effects ; Synaptic Transmission/*drug effects
    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)
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