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  • Articles  (10)
  • Kinetics  (10)
  • American Association for the Advancement of Science (AAAS)  (10)
  • Blackwell Publishing Ltd
  • 1975-1979  (10)
  • 1
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    Intercellular communication in pancreatic islet monolayer cultures: a microfluorometric study (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-05-25
    Description: Single islet cells in monolayer cultures of neonatal rat pancreas were microinjected with fluorescein and scanned topographically by microfluorometry. Fluorescein spread from an injected islet cell directly into neighboring islet cells, and, in the presence of 16.7 millimolar glucose, significantly more islet cells communicated with the injected cell than in glucose-free medium. Islet cells were also microinjected with glycolytic substrates and activators that produced transient changes in cellular levels of reduced pyridine nucleotides-nicotinamide adenine dinucleotide and nicotinamide adenine dinucleotide phosphate [NAD(P)H]. Changes in NAD(P)H fluorescence were observed in islet cells incubated first for 18 hours in very low glucose concentrations and then in a glucose-free medium and injected with glycolytic substrates and activators; however, little change of fluorescence occurred in adjacent islet cells. In contrast, after adding 16.7 millimolar glucose to the medium, injection of glycolytic substrates and activators produced transient changes in NAD(P)H fluorescence in the injected cell and in neighboring cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kohen, E -- Kohen, C -- Thorell, B -- Mintz, D H -- Rabinovitch, A -- New York, N.Y. -- Science. 1979 May 25;204(4395):862-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/35828" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Communication/drug effects ; Fluoresceins ; Glucose/pharmacology ; Glycolysis ; Islets of Langerhans/cytology/*physiology ; Kinetics ; NAD/metabolism ; NADP/metabolism ; Rats ; Spectrometry, Fluorescence
    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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    A structural model for the kinetic behavior of hemoglobin (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-11-30
    Description: The tertiary structures of all liganded hemoglobins in the R state differ in detail. Steric hindrance arising from nonbonded ligand-globin interactions affects the binding of ligands such as CO and cyanide which preferentially form linear axial complexes to heme; these ligands bind in a strained off-axis configuration. Ligands such as O2 and NO, which preferentially form bent complexes, encounter less steric hindrance and can bind in their (preferred) unstrained configuration. Linear complexes distort the ligand pockets in the R state (and by inference, in the T state) more than bent complexes. These structural differences between linear and bent complexes are reflected in the kinetic behavior of hemoglobin. Structural interpretation of this kinetic behavior indicates that the relative contributions of nonbonded ligand-globin interactions and nonbonded heme interactions to transition state free energies differ for linear and bent ligands. The relative contributions of these interactions to the free energy of cooperativity may also differ for linear and bent ligands. Thus the detailed molecular mechanism by which the affinity of heme is regulated differs for different ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moffat, K -- Deatherage, J F -- Seybert, D W -- New York, N.Y. -- Science. 1979 Nov 30;206(4422):1035-42.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/493990" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Animals ; Heme/*metabolism ; Hemoglobins/metabolism ; Horses ; Kinetics ; Ligands ; Oxygen/*metabolism ; Oxyhemoglobins/*metabolism ; Protein Conformation ; Stereoisomerism ; Structure-Activity Relationship
    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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    Potassium activation associated with intraneuronal free calcium (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-04-28
    Description: Relations between calcium entry and activation of a calcium-dependent outward current during depolarization were examined under voltage clamp in dorid giant neurons injected with the calcium-sensitive photoprotein aequorin. Activation kinetics and amplitude of the slow calcium-dependent component were both found to be related to the rate and extent of free calcium accumulation and to the electromotive force acting on potassium ions, independent of the calcium activation kinetics. This indicates that the activation of the calcium-dependent outward current is more closely related to the transient intracellular accumulation of free calcium ions than to the movement of calcium through the plasma membrane during depolarization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eckert, R -- Tillotson, D -- New York, N.Y. -- Science. 1978 Apr 28;200(4340):437-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/644308" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*metabolism ; In Vitro Techniques ; Kinetics ; Membrane Potentials ; Mollusca ; Neurilemma/physiology ; Neurons/*metabolism ; Potassium/*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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  • 4
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    Entry of insulin into human cultured lymphocytes: electron microscope autoradiographic analysis (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-11-17
    Description: Electron microscope autoradiographs were prepared of IM-9 human cultured lymphocytes incubated with iodine-125-labeled insulin. With the use of [125I]insulin and Ilford L-4 emulsion, the technique had a resolution half-distance of approximately 0.085 micrometer. Autoradiographs revealed a time-dependent entry of insulin into the cell interior that was maximal after 30 minutes of incubation. At this time point nearly 40 percent of the [125I]insulin was in the interior of the cell at a distance 1 micrometer or greater from the plasma membrane. Grain distribution and volume density analyses revealed that the intracellular insulin was concentrated in the endoplasmic reticulum and nuclear membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldfine, I D -- Jones, A L -- Hradek, G T -- Wong, K Y -- Mooney, J S -- New York, N.Y. -- Science. 1978 Nov 17;202(4369):760-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/715440" target="_blank"〉PubMed〈/a〉
    Keywords: Autoradiography ; Biological Transport ; Cell Nucleus/metabolism ; Cells, Cultured ; Endoplasmic Reticulum/metabolism ; Humans ; Insulin/*metabolism ; Kinetics ; Lymphocytes/*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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    Slow axonal transport of neurofilament proteins: impairment of beta,beta'-iminodipropionitrile administration (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-11-10
    Description: beta,beta'-Iminodipropionitrile (IDPN) administration prevented normal slow axonal transport of [35S]methionine- or [3H]leucine-labeled proteins in rat sciatic motor axons. Ultrastructural and electrophoretic studies showed that the neurofilament triplet proteins in particular were retained within the initial 5 millimeters of the axons, resulting in neurofilament-filled axonal swellings. Fast anterograde and retrograde axonal transport were not affected. The IDPN thus selectively impaired slow axonal transport. The neurofibrillary pathology in this model is the result of the defective slow transport of neurofilaments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Griffin, J W -- Hoffman, P N -- Clark, A W -- Carroll, P T -- Price, D L -- New York, N.Y. -- Science. 1978 Nov 10;202(4368):633-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/81524" target="_blank"〉PubMed〈/a〉
    Keywords: Axonal Transport/*drug effects ; Kinetics ; Molecular Weight ; Nerve Tissue Proteins/*metabolism ; Neurofibrils/metabolism/ultrastructure ; Nitriles/*pharmacology/toxicity ; Sciatic Nerve/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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  • 6
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    Rod-cone dysplasia in Irish setters: a defect in cyclic GMP metabolism in visual cells (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-09-22
    Description: An abnormality in retinal guanosine 3,5-monophosphate (cyclic GMP) metabolism is demonstrated in the inherited rod-cone dysplasis of Irish Setter dogs. Affected visual cells are deficient in cyclic GMP phosphodiesterase activity and have elevated levels of cyclic GMP. The biochemical abnormalities observed in affected retinas of Irish Setters are similar to those in the retinas of mice with inherited retinal degeneration before visual cell degeneration begins. A defect in cyclic GMP metabolism may be characteristic of early-onset degenerative diseases of the retina, possibly including those that affect humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aquirre, G -- Farber, D -- Lolley, R -- Fletcher, R T -- Chader, G J -- New York, N.Y. -- Science. 1978 Sep 22;201(4361):1133-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/210508" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-GMP Phosphodiesterases/*deficiency ; Animals ; Cell Differentiation ; Chromosome Aberrations/genetics/metabolism/pathology/veterinary ; Chromosome Disorders ; Cyclic GMP/*metabolism ; Dog Diseases/genetics/*metabolism/pathology ; Dogs ; Kinetics ; Mice ; Photoreceptor Cells/metabolism/pathology ; Retina/enzymology/*metabolism/pathology ; Retinal Degeneration/genetics/metabolism/pathology/*veterinary
    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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    Diffusion-like process can account for protein secretion by the pancreas (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-06-15
    Description: When fluid secretion by the pancreas was mechanically blocked, amylase secretion into the duct ceased. When flow was reduced in a graded fashion by the application of a back pressure, amylase output was reduced proportionately and amylase concentration in secretion was maintained constant. Thus, the secretion of digestive enzyme from the cell into the duct appears to be dependent upon the concentration of enzyme in the duct system. This behavior is most simply explained by diffusion-like (concentration dependent, bidirectional) fluxes of digestive enzyme across the plasma membrane. A unidirectional process, such as exocytosis, whose rate should be unaffected by fluid flow, cannot readily explain these results.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Isenman, L D -- Rothman, S S -- New York, N.Y. -- Science. 1979 Jun 15;204(4398):1212-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/451566" target="_blank"〉PubMed〈/a〉
    Keywords: Amylases/*secretion ; Animals ; Biological Transport ; Diffusion ; Exocytosis ; Hydrostatic Pressure ; Kinetics ; Pancreas/*secretion ; Rabbits ; Water-Electrolyte Balance
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    Electronic ISSN: 1095-9203
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  • 8
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    Membrane enzymes: artifacts in Arrhenius plots due to temperature dependence of substrate-binding affinity (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-02-24
    Description: For the membrane sodium-stimulated magnesium-adenosinetriphosphatase of Acholeplasma laidlawii B both the Vmax and Km values in the Michaelis equation very strongly with temperature. Simulations of Arrhenius plots show that an enzyme with a temperature-dependent Km can yield a variety of Arrhenius plot artifacts, most notably erroneous "breaks," if activity is assayed at a fixed substrate concentration.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Silvius, J R -- Read, B D -- McElhaney, R N -- New York, N.Y. -- Science. 1978 Feb 24;199(4331):902-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/146257" target="_blank"〉PubMed〈/a〉
    Keywords: Acholeplasma laidlawii/enzymology ; Adenosine Triphosphatases/*metabolism ; Adenosine Triphosphate/metabolism ; Fatty Acids/pharmacology ; Kinetics ; Magnesium/metabolism ; Membrane Proteins/metabolism ; Membranes/*enzymology ; Temperature ; Thermodynamics
    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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    beta1- and beta2-Adrenergic receptors in rat cerebral cortex are independently regulated (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-05-25
    Description: Repeated administration of the tricyclic antidepressant desmethylimipramine to adult rats for 10 days caused a 40% decrease in the density of beta1-adrenergic receptors in the cerebral cortex but had no effect on the density of beta2-adrenergic receptors. Conversely, destruction of noradrenergic neurons by administration of 6-hydroxydopamine to neonatal rats caused a 64% increase in the density of beta1-adrenergic receptors in adult cerebral cortex with no change in the density of beta2-adrenergic receptors. These results suggest that the beta-adrenergic receptors in rat cortex involved in neuronal function are primarily of the beta1 subtype.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Minneman, K P -- Dibner, M D -- Wolfe, B B -- Molinoff, P B -- New York, N.Y. -- Science. 1979 May 25;204(4395):866-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/35829" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenergic beta-Agonists/metabolism ; Animals ; Binding, Competitive ; Cerebral Cortex/*metabolism ; Cyclic AMP/metabolism ; Desipramine/pharmacology ; Hydroxydopamines/pharmacology ; Kinetics ; Rats ; Receptors, Adrenergic/*metabolism ; Receptors, Adrenergic, beta/drug effects/*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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    Acridine araphanes: a new class of probe molecules for biological systems (1979)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1979-09-21
    Description: The bis-acridine ring system forms the basis for new biophysical probes of novel stereochemistry. Spectral data indicate that certain alkylene bridged bis-9-aminoacridines have a parallel plane conformation of predictable interplane distance. The parallel plane conformation is independent of solvent and thus is different from nucleic acid systems. This stable conformation allows these compounds to be used as sensitive "rulers" for describing binding site geometry in cholinergic enzymes and in the delineation of the mechanism of allosteric control in acetylcholinesterase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Himel, C M -- Taylor, J L -- Pape, C -- Millar, D B -- Christopher, J -- Kurlansik, L -- New York, N.Y. -- Science. 1979 Sep 21;205(4412):1277-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/472743" target="_blank"〉PubMed〈/a〉
    Keywords: *Acetylcholinesterase/metabolism ; *Acridines ; Binding Sites ; Kinetics ; Molecular Conformation ; Phosphorylation ; Protein Conformation ; Spectrophotometry, Ultraviolet
    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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