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  • Kinetics
  • American Association for the Advancement of Science (AAAS)  (20)
  • Annual Reviews
  • Blackwell Publishing Ltd
  • Cambridge University Press
  • Institute of Physics
  • 1980-1984  (20)
  • 1970-1974
  • 1930-1934
  • 1925-1929
  • 1984  (20)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (20)
  • Annual Reviews
  • Blackwell Publishing Ltd
  • Cambridge University Press
  • Institute of Physics
  • +
Years
  • 1980-1984  (20)
  • 1970-1974
  • 1930-1934
  • 1925-1929
Year
  • 1
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    American Association for the Advancement of Science (AAAS)
    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
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  • 2
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    American Association for the Advancement of Science (AAAS)
    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
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  • 3
    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
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  • 4
    Publication Date: 1984-02-10
    Description: Ultraviolet irradiation of rat dendritic cells completely abrogated their allostimulatory capacity in a mixed lymphocyte reaction. Rat islets of Langerhans similarly irradiated remained hormonally functional when transplanted into syngeneic diabetic rats. Allogeneic transplantation across a major histocompatibility barrier of islets initially treated in vitro with ultraviolet irradiation resulted in prolonged allograft survival without the use of any immunosuppressive agents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lau, H -- Reemtsma, K -- Hardy, M A -- New York, N.Y. -- Science. 1984 Feb 10;223(4636):607-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6420888" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Survival/radiation effects ; Dose-Response Relationship, Radiation ; Islets of Langerhans/radiation effects ; *Islets of Langerhans Transplantation ; Kinetics ; Rats ; Rats, Inbred Lew ; Transplantation, Homologous ; Transplantation, Isogeneic ; *Ultraviolet Rays
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  • 5
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    American Association for the Advancement of Science (AAAS)
    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
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  • 6
    Publication Date: 1984-02-10
    Description: 3-Aminobenzamide and benzamide, purported to be specific inhibitors of the synthesis of poly(adenosine diphosphate-ribose), were used to elucidate possible functions of this biopolymer. These compounds, at frequently used experimental concentrations, not only inhibited the action of poly(adenosine diphosphate-ribose) synthetase but also affected cell viability, glucose metabolism, and DNA synthesis. Thus, the usefulness of 3-aminobenzamide and benzamide may be severely restricted by the difficulty of finding a dose small enough to inhibit the synthetase without producing additional metabolic effects.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milam, K M -- Cleaver, J E -- New York, N.Y. -- Science. 1984 Feb 10;223(4636):589-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6420886" target="_blank"〉PubMed〈/a〉
    Keywords: Benzamides/*toxicity ; Cell Line ; DNA Replication/drug effects ; Humans ; Kinetics ; Lymphocytes ; Nucleoside Diphosphate Sugars/*biosynthesis ; Poly Adenosine Diphosphate Ribose/*biosynthesis ; Poly(ADP-ribose) Polymerases/metabolism ; Structure-Activity Relationship
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  • 7
    Publication Date: 1984-05-11
    Description: Arabinosylcytosine, a compound that inhibits DNA synthesis in rapidly dividing cells, stimulates fetal hemoglobin in adult baboons and produces significant perturbations in the pools of erythroid progenitors. It appears that changes in the kinetics of erythroid cell differentiation rather than direct action on the gamma genes underlie stimulation of fetal hemoglobin in the adult animals in vivo. These results also suggest that chemotherapeutic agents selected for their low carcinogenic or mutagenic potential could be used for therapeutic induction of fetal hemoglobin in patients with sickle cell anemia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Papayannopoulou, T -- Torrealba de Ron, A -- Veith, R -- Knitter, G -- Stamatoyannopoulos, G -- GM 15253/GM/NIGMS NIH HHS/ -- HL-07093/HL/NHLBI NIH HHS/ -- HL-20899/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1984 May 11;224(4649):617-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6200940" target="_blank"〉PubMed〈/a〉
    Keywords: Anemia, Sickle Cell/drug therapy ; Animals ; Cell Differentiation/*drug effects ; Cytarabine/*pharmacology/therapeutic use ; Erythropoiesis/*drug effects ; Fetal Hemoglobin/*biosynthesis ; Kinetics ; Papio ; Reticulocytes/drug effects
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  • 8
    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
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  • 9
    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
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-02-17
    Description: Neurons process and transmit information in the form of electrical signals. Their electrical excitability is due to the presence of voltage-sensitive ion channels in the neuronal plasma membrane. In recent years, the voltage-sensitive sodium channel of mammalian brain has become the first of these important neuronal components to be studied at the molecular level. This article describes the distribution of sodium channels among the functional compartments of the neuron and reviews work leading to the identification, purification, and characterization of this membrane glycoprotein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Catterall, W A -- New York, N.Y. -- Science. 1984 Feb 17;223(4637):653-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6320365" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/metabolism ; Cell Membrane/metabolism ; Electric Organ ; Electrophorus ; Ion Channels/*metabolism ; Kinetics ; Macromolecular Substances ; Membrane Proteins/genetics/isolation & purification ; Molecular Weight ; Muscles/metabolism ; Nerve Tissue Proteins/isolation & purification ; Neurons/*metabolism/physiology ; Neurotoxins/pharmacology ; Protein Processing, Post-Translational ; Sodium/*metabolism
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  • 11
    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
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-04-20
    Description: The spatial variation of changes in intracellular calcium ions were studied with a one-dimensional scanning microphotometer. Changes in intracellular calcium were measured with a metallochromic dye, arsenazo III. Both the magnitude and the kinetics of changes in calcium were dramatically different in different regions of a cell. In Limulus ventral photoreceptors the maximum change was probably restricted to the rhabdomeric lobe.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harary, H H -- Brown, J E -- EY0914/EY/NEI NIH HHS/ -- EY0915/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1984 Apr 20;224(4646):292-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6710144" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arsenazo III/metabolism ; Calcium/*metabolism ; Cytosol/metabolism ; Diffusion ; Horseshoe Crabs/*metabolism ; Kinetics ; Light ; Photoreceptor Cells/*metabolism ; Spectrophotometry
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  • 13
    Publication Date: 1984-02-10
    Description: Regression of the fetal rat Mullerian duct in vitro was stimulated by sodium fluoride in the absence of Mullerian inhibiting substance. The action of Mullerian inhibiting substance was inhibited by sodium vanadate, adenosine 5'-triphosphate, and several related nucleotides in the presence of manganese ions. Epidermal growth factor specifically inhibited the substance, but only with manganese ions present. Insulin, platelet-derived growth factor, and nerve growth factor had no effect. These results suggest that dephosphorylation of membrane proteins mediates the action of Mullerian inhibiting substance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hutson, J M -- Fallat, M E -- Kamagata, S -- Donahoe, P K -- Budzik, G P -- CA-17393/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1984 Feb 10;223(4636):586-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6607531" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Mullerian Hormone ; Cations, Divalent ; Dimethyl Sulfoxide/pharmacology ; Epidermal Growth Factor/pharmacology ; Female ; *Glycoproteins ; *Growth Inhibitors ; Kinetics ; Male ; Membrane Proteins/metabolism ; Mullerian Ducts/drug effects/*physiology ; Phosphorylation ; Pregnancy ; Rats ; Sodium Fluoride/pharmacology ; Testicular Hormones/*physiology ; Vanadates ; Vanadium/pharmacology
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  • 14
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    American Association for the Advancement of Science (AAAS)
    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
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  • 15
    Publication Date: 1984-05-11
    Description: Arachidonate and other unsaturated long-chain fatty acids were found to activate protein kinase C from human neutrophils. Kinase activation by arachidonate required calcium and was enhanced by diolein but did not require exogenous phosphatidylserine. Submaximal levels of arachidonate also enhanced the affinity of the kinase for calcium during activation by phosphatidylserine. Thus the release of arachidonate, which is triggered in many cell types by ligand-receptor interactions, could play a second messenger role in the regulation of cellular function by activation of protein kinase C.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McPhail, L C -- Clayton, C C -- Snyderman, R -- 5PO1CA29589/CA/NCI NIH HHS/ -- 5RO-1DEO3738/DE/NIDCR NIH HHS/ -- New York, N.Y. -- Science. 1984 May 11;224(4649):622-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6231726" target="_blank"〉PubMed〈/a〉
    Keywords: Arachidonic Acid ; Arachidonic Acids/pharmacology ; Dose-Response Relationship, Drug ; Enzyme Activation ; Fatty Acids, Unsaturated/pharmacology/*physiology ; Humans ; Kinetics ; Neutrophils/enzymology ; Phosphatidylserines/pharmacology ; Protein Kinase C ; Protein Kinases/*metabolism
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  • 16
    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
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  • 17
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-04-20
    Description: Human epidermoid carcinoma A431 cells in culture produce a soluble 105-kilodalton protein which, by the criteria of epidermal growth factor (EGF) binding, recognition by monoclonal and polyclonal antibodies to the EGF receptor, amino-terminal sequence analysis and carbohydrate content, is related to the cell surface domain of the EGF receptor. The high rate of production and the finding that with biosynthetic labeling the specific activity of this 105-kilodalton protein exceeds that of the intact receptor indicate that it is not derived from membrane-bound mature receptor but is separately produced by the cell. These cells thus separately synthesize an EGF receptor that is inserted into the membrane and an EGF receptor-related protein that is secreted.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weber, W -- Gill, G N -- Spiess, J -- AM13149/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1984 Apr 20;224(4646):294-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6324343" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal/immunology ; Carbohydrates/analysis ; Carcinoma, Squamous Cell/*metabolism ; Cell Line ; Epidermal Growth Factor/metabolism ; Glycoproteins/analysis/*biosynthesis ; Humans ; Kinetics ; Molecular Weight ; Receptor, Epidermal Growth Factor ; Receptors, Cell Surface/analysis/immunology/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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  • 18
    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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  • 19
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1984-02-10
    Description: The resistance of the infectious agent of scrapie disease to sterilization at 100 degrees or 121 degrees C is reputed to be inconsistent with the structure of conventional viruses. However, in kinetic studies the majority of hamster scrapie strain 263K infectivity was (like that of previously characterized viruses) rapidly inactivated at temperatures of 100 degrees C or greater. Small resistant subpopulations remained. Similar heat-resistant subpopulations were observed at 60 degrees C for phage lambda but only in the presence of brain homogenate. Brain homogenate may also confer stability to small subfractions of scrapie infectivity. Such refractory subpopulations cannot be used to make structural inferences that are properly obtained from the behavior of the majority population as revealed in the initial inactivation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rohwer, R G -- New York, N.Y. -- Science. 1984 Feb 10;223(4636):600-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6420887" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/microbiology ; Cricetinae ; *Hot Temperature ; Kinetics ; Prions/*growth & development ; Species Specificity ; Sterilization/methods
    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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  • 20
    Publication Date: 1984-03-16
    Description: 5-Amino-4-imidazolecarboxamide riboside triphosphate (ZTP) is thought to play a regulatory role in cellular metabolism. Unlike other nucleoside triphosphates, ZTP is synthesized in a one-step reaction in which the pyrophosphate group of 5-phosphoribosyl-l-pyrophosphate is transferred to the riboside monophosphate (ZMP) in a reaction catalyzed by 5-phosphoribosyl-l-pyrophosphate synthetase; reversal of this reaction leads to dephosphorylation of ZTP to ZMP. This unusual route of synthesis (and catabolism) of ZTP may be important in defining its metabolic effects in the cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sabina, R L -- Holmes, E W -- Becker, M A -- AM12413/AM/NIADDK NIH HHS/ -- AM28554/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1984 Mar 16;223(4641):1193-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6199843" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Aminoimidazole Carboxamide/analogs & derivatives/*biosynthesis/pharmacology ; Animals ; Cell Line ; Cricetinae ; Imidazoles/*biosynthesis ; Kinetics ; Phosphoribosyl Pyrophosphate/metabolism ; Phosphorylation ; Ribonucleosides/pharmacology ; Ribonucleotides/*biosynthesis ; Ribose-Phosphate Pyrophosphokinase/metabolism ; Substrate Specificity
    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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