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  • Articles  (136)
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  • Kinetics  (136)
  • 1980-1984  (136)
  • Natural Sciences in General  (136)
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  • Articles  (136)
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  • 1
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    Novel pharmacology of substance K-binding sites: a third type of tachykinin receptor (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-23
    Description: The tachykinins are a family of peptides with the carboxyl terminal amino acid sequence Phe-X-Gly-Leu-Met-NH2. Three major mammalian tachykinins have been identified--substance K, neuromedin K, and substance P--but only two tachykinin receptors have been postulated. Three tachykinins were labeled with radioiodinated Bolton-Hunter reagent and their binding characteristics were determined in crude membrane suspensions from several tissues. In cerebral cortex labeled eledoisin exhibited high-affinity binding that was inhibited by tachykinins in a manner indicating a definitive SP-E receptor site. In gastrointestinal smooth muscle and bladder, high-affinity binding of labeled substance P was inhibited in a pattern indicating a definitive SP-P site. In intestinal smooth muscle and bladder, however, labeled substance K and labeled eledoisin were both bound in a pattern indicating a preference for substance K itself. The results suggest the existence of three distinct types of tachykinin receptors: SP-P, SP-E, and SP-K.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Buck, S H -- Burcher, E -- Shults, C W -- Lovenberg, W -- O'Donohue, T L -- New York, N.Y. -- Science. 1984 Nov 23;226(4677):987-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6095447" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding, Competitive ; Cell Membrane/metabolism ; Cerebral Cortex/*metabolism ; Duodenum/*metabolism ; Guinea Pigs ; Intestine, Small/*metabolism ; Kinetics ; Mice ; Organ Specificity ; Peptides/*metabolism ; Rats ; Receptors, Neurokinin-2 ; Receptors, Neurotransmitter/*metabolism ; *Receptors, Tachykinin ; Species Specificity ; Tachykinins ; Urinary Bladder/*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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  • 2
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    Modulation of the metastatic activity of melanoma cells by laminin and fibronectin (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-23
    Description: Metastatic mouse melanoma cells have a high affinity for the basement membrane and the ability to degrade it; these properties may allow tumor cells to invade the membrane and disseminate. In this study it was found that the metastatic potential of mouse melanoma cells varied when the cells were exposed in culture to fibronectin or laminin. After removal of fibronectin or exposure to laminin, the cells had an increased affinity for basement membrane collagen, were more invasive of basement membranes in vitro, and produced more lung colonies in vivo. These changes are correlated with and may be due to an increase in the laminin-binding capacity of the tumor cell surface.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Terranova, V P -- Williams, J E -- Liotta, L A -- Martin, G R -- New York, N.Y. -- Science. 1984 Nov 23;226(4677):982-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6505678" target="_blank"〉PubMed〈/a〉
    Keywords: Amnion/physiology ; Animals ; Cell Division/drug effects ; Cell Line ; Female ; Fibronectins/*pharmacology ; Humans ; Immune Sera ; Kinetics ; Laminin/*pharmacology ; Melanoma/*pathology ; Mice ; Neoplasm Metastasis/*pathology ; Pregnancy
    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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  • 3
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    Benzodiazepine receptor synthesis and degradation by neurons in culture (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-16
    Description: The benzodiazepine-gamma-aminobutyric acid receptor complex was used to study functional receptor synthesis and degradation in primary cultures of neurons. Fifty percent of the receptors turned over with an unusually rapid half-life (4 hours); this was followed by a second, slower phase (32 hours). These results provide the basis for elucidating the mechanism by which neurons derived from the central nervous system control neurotransmitter receptor number, an important problem in cellular neurobiology. The findings may be of significance in the study of neurological and psychiatric disorders.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Borden, L A -- Czajkowski, C -- Chan, C Y -- Farb, D H -- New York, N.Y. -- Science. 1984 Nov 16;226(4676):857-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6093257" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Chick Embryo ; Flunitrazepam/metabolism ; Half-Life ; Kinetics ; Neurons/*metabolism ; Receptors, GABA-A/biosynthesis/*metabolism ; Spinal Cord/cytology ; gamma-Aminobutyric Acid/physiology
    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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    Chemical mutation of enzyme active sites (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-02
    Description: New active sites can be introduced into naturally occurring enzymes by the chemical modification of specific amino acid residues with the use of appropriately designed coenzyme analogs. The resultant semisynthetic enzymes can have catalytic activities very different from those of the corresponding native enzymes. For example, papain has been converted into a highly effective oxidoreductase by covalent modification of the sulfhydryl group of the active site cysteine residue (Cys25) with flavins such as 8-bromoacetyl-10-methylisoalloxazine. Thus, it is now possible to enhance the catalytic versatility of existing enzymes through the process of "chemical mutation" of the active site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, E T -- Lawrence, D S -- New York, N.Y. -- Science. 1984 Nov 2;226(4674):505-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6238407" target="_blank"〉PubMed〈/a〉
    Keywords: Anaerobiosis ; *Binding Sites ; Catalysis ; Chemical Phenomena ; *Chemistry ; Chymotrypsin ; Enzymes/*chemical synthesis ; Flavins ; Kinetics ; NAD/metabolism ; Niacinamide/analogs & derivatives ; Oxidation-Reduction ; Papain ; Stereoisomerism ; Toluene/analogs & derivatives/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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  • 5
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    Cyclophilin: a specific cytosolic binding protein for cyclosporin A (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-02
    Description: Cyclophilin, a specific cytosolic binding protein responsible for the concentration of the immunosuppressant cyclosporin A by lymphoid cells, was purified to homogeneity from bovine thymocytes. Cation-exchange high-performance liquid chromatography resolved a major and minor cyclophilin species that bind cyclosporin A with a dissociation constant of about 2 X 10(-7) moles per liter and specific activities of 77 and 67 micrograms per milligram of protein, respectively. Both cyclophilin species have an apparent molecular weight of 15,000, an isoelectric point of 9.6, and nearly identical amino acid compositions. A portion of the NH2-terminal amino acid sequence of the major species was determined. The cyclosporin A-binding activity of cyclophilin is sulfhydryl dependent, unstable at 56 degrees C and at pH 4 or 9.5, and sensitive to trypsin but not to chymotrypsin digestion. Cyclophilin specifically binds a series of cyclosporin analogs in proportion to their activity in a mixed lymphocyte reaction. Isolation of cyclophilin from the cytosol of thymocytes suggests that the immunosuppressive activity of cyclosporin A is mediated by an intracellular mechanism, not by a membrane-associated mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Handschumacher, R E -- Harding, M W -- Rice, J -- Drugge, R J -- Speicher, D W -- New York, N.Y. -- Science. 1984 Nov 2;226(4674):544-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6238408" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/*isolation & purification/metabolism ; Cattle ; Chromatography, High Pressure Liquid ; Cyclosporins/*metabolism ; Electrophoresis, Polyacrylamide Gel ; Humans ; Isoelectric Point ; Kinetics ; Lymphocyte Culture Test, Mixed ; Mice ; Molecular Weight ; Peptidylprolyl Isomerase
    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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    Disulfide bond engineered into T4 lysozyme: stabilization of the protein toward thermal inactivation (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-02
    Description: By recombinant DNA techniques, a disulfide bond was introduced at a specific site in T4 lysozyme, a disulfide-free enzyme. This derivative retained full enzymatic activity and was more stable toward thermal inactivation than the wild-type protein. The derivative, T4 lysozyme (Ile3----Cys), was prepared by substituting a Cys codon for an Ile codon at position 3 in the cloned lysozyme gene by means of oligonucleotide-dependent, site-directed mutagenesis. The new gene was expressed in Escherichia coli under control of the (trp-lac) hybrid tac promoter, and the protein was purified. Mild oxidation generated a disulfide bond between the new Cys3 and Cys97, one of the two unpaired cysteines of the native molecule. Oxidized T4 lysozyme (Ile3----Cys) exhibited specific activity identical to that of the wild-type enzyme when measured at 20 degrees C in a cell-clearing assay. The cross-linked protein was more stable than the wild type during incubation at elevated temperatures as determined by recovered enzymatic activity at 20 degrees C.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perry, L J -- Wetzel, R -- New York, N.Y. -- Science. 1984 Nov 2;226(4674):555-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6387910" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; DNA, Recombinant/metabolism ; Escherichia coli/enzymology ; *Genetic Engineering ; Kinetics ; Muramidase/*genetics/metabolism ; Protein Denaturation
    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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    Optical measurements of extracellular calcium depletion during a single heartbeat (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-10-12
    Description: The impermeant dye antipyrylazo III was used to measure depletion of extracellular calcium and net influx of calcium through the sarcolemma during the cardiac action potential. It was found that calcium entry occurs continuously during the action potential and is under direct control of the membrane potential. The inotropic action of epinephrine is accompanied by increased influx of calcium, while strophanthidin enhances the twitch without altering calcium influx during the action potential.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cleemann, L -- Pizarro, G -- Morad, M -- HL16152/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1984 Oct 12;226(4671):174-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6091269" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Calcium/*metabolism ; Epinephrine/pharmacology ; Extracellular Space/*metabolism ; Ion Channels ; Kinetics ; *Myocardial Contraction/drug effects ; Myocardium/*metabolism ; Naphthalenesulfonates ; Ranidae ; Sarcolemma/*metabolism ; Spectrophotometry ; Stimulation, Chemical ; Strophanthidin/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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    Inhibition of human estrogen synthetase (aromatase) by flavones (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-09-07
    Description: Several naturally occurring and synthetic flavones were found to inhibit the aromatization of androstenedione and testosterone to estrogens catalyzed by human placental and ovarian microsomes. These flavones include (in order of decreasing potency) 7,8-benzoflavone, chrysin, apigenin, flavone, flavanone, and quercetin; 5,6-benzoflavone was not inhibitory. 7,8-Benzoflavone and chrysin were potent competitive inhibitors and induced spectral changes in the aromatase cytochrome P-450 indicative of substrate displacement. Flavones may thus compete with steroids in their interaction with certain monooxygenases and thereby alter steroid hormone metabolism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kellis, J T Jr -- Vickery, L E -- AM1005/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1984 Sep 7;225(4666):1032-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6474163" target="_blank"〉PubMed〈/a〉
    Keywords: Androstenedione/*metabolism ; *Aromatase Inhibitors ; Benzoflavones/metabolism/pharmacology ; Binding Sites ; Binding, Competitive ; Female ; Flavonoids/metabolism/*pharmacology ; Humans ; Kinetics ; Microsomes/enzymology ; Ovary/*enzymology ; Oxidoreductases/*antagonists & inhibitors ; Placenta/*enzymology ; Pregnancy ; Testosterone/*metabolism ; beta-Naphthoflavone
    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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  • 9
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    Inhibition of cholesterol crystal formation by apolipoproteins in supersaturated model bile (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-08-03
    Description: Apolipoproteins A-1 and A-2 were purified from human plasma. At concentrations present in human bile these proteins prolonged the nucleation time of cholesterol monohydrate crystals when added to model systems of supersaturated bile. In contrast, apolipoprotein C-3 and other serum proteins did not have this effect. Also, when human gallbladder bile was fractionated by gel filtration chromatography, apolipoproteins A-1 and A-2 were among the proteins present in a fraction of bile enriched in potent inhibitors of cholesterol crystal nucleation. These findings suggest that apolipoproteins A-1 and A-2 in supersaturated human gallbladder bile could inhibit the rate of formation of solid cholesterol crystals and thus help to prevent spontaneous cholesterol gallstone formation in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kibe, A -- Holzbach, R T -- LaRusso, N F -- Mao, S J -- AM-17562/AM/NIADDK NIH HHS/ -- AM-24031/AM/NIADDK NIH HHS/ -- HL-32317/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1984 Aug 3;225(4661):514-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6429856" target="_blank"〉PubMed〈/a〉
    Keywords: Apolipoprotein A-I ; Apolipoprotein A-II ; Apolipoproteins/*blood ; Bile/*physiology ; Cholesterol/*metabolism ; Crystallization ; Gallbladder/physiology ; Humans ; Kinetics ; Lipoproteins, HDL/*blood ; Models, Biological
    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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    Influence of spaceflight on erythrokinetics in man (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-07-13
    Description: A significant postflight reduction in the circulating red cell mass has been observed in both the American and Soviet manned programs. The mechanism and etiology of this loss were studied in blood samples from the four payload crewmen of Spacelab 1 taken before, during, and after flight. These samples and samples from control groups on the ground were analyzed for selected hematological and biochemical parameters, which were chosen on the basis of data previously collected, the restraints imposed by the use of human subjects, and the guidelines established for the first Spacelab mission. Twenty-two hours after weightless exposure, there was an increase in hemoglobin and hematocrit. On day 7 in flight, the hemoglobin and hematocrit remained high and there was a slight decrease in reticulocyte number. On landing, red cell mass, plasma volume, hematocrit, and reticulocyte number were decreased. Throughout the 2-week postflight sampling period, hemoglobin, hematocrit, and reticulocyte number remained below the preflight value. Since this crew was not exposed to 100 percent oxygen these results are viewed as evidence that other spaceflight factors cause the measured red cell mass reduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leach, C S -- Johnson, P C -- New York, N.Y. -- Science. 1984 Jul 13;225(4658):216-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6729477" target="_blank"〉PubMed〈/a〉
    Keywords: Erythrocyte Count ; Erythrocyte Volume ; Erythrocytes/*physiology ; Erythropoiesis ; Erythropoietin/blood ; Hematocrit ; Hemoglobins/analysis ; Humans ; Kinetics ; Reticulocytes ; *Space Flight
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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