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  • *Biological Evolution
  • Binding Sites
  • American Association for the Advancement of Science (AAAS)  (11)
  • 2005-2009
  • 1975-1979  (11)
  • 1979  (11)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (11)
Years
  • 2005-2009
  • 1975-1979  (11)
Year
  • 1
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    Time-resolved europium(III) excitation spectroscopy: a luminescence probe of metal ion binding sites (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-12-07
    Description: A laser-induced luminescence technique is introduced for probing the structure and equilibria of lanthanide complexes and lanthanide ion binding to macromolecules. The method involves the excitation of the 7F0 leads to 5D0 transition between nondegenerate levels in the europium(III) ion by means of an intense pulsed dye laser source. Excitation profits obtained by scanning the laser through the transition region reveal distinct peaks characteristic of individual europium(III) ion environments. The technique may be used to characterize the species present in complex equilibria in solution or to study europium(III) binding to macromolecules. Distinct europium(III) binding sites in thermolysin with long and short excited state lifetimes are observed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Horrocks, W D Jr -- Sudnick, D R -- New York, N.Y. -- Science. 1979 Dec 7;206(4423):1194-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/505007" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; *Europium ; Luminescence ; Protein Binding ; Spectrum Analysis/methods ; Thermolysin
    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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    Radioimmunoassay of the insulin receptor: a new probe of receptor structure and function (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-02-09
    Description: A sensitive and specific radioimmunoassay for the insulin receptor has been developed employing receptor autoantibodies from the serum of a patient with insulin-resistant diabetes. The assay detects insulin binding sites at concentrations as low as 0.1 nanomolar; distinguishes between receptors originating from human placental membranes, human lymphoblastoid cells, and mouse liver membranes; and measures the receptor independently of its binding function. Down-regulation, or loss of binding after exposure to insulin, is associated with loss of immunoreactive receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harrison, L C -- Flier, J -- Itin, A -- Kahn, C R -- Roth, J -- New York, N.Y. -- Science. 1979 Feb 9;203(4380):544-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/83675" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigen-Antibody Reactions ; Binding Sites ; Binding Sites, Antibody ; Epitopes ; Female ; Humans ; Liver/analysis ; Lymphocytes/analysis ; Mice ; Placenta/analysis ; Pregnancy ; Radioimmunoassay/methods ; Receptor, Insulin/analysis/*immunology ; Solubility
    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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    Heterogeneity of vertebrate luteinizing hormone-releasing hormone (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-10-05
    Description: Radioimmunoassay and chromatography analyses of hypothalamic luteinizing hormone-releasing hormone (LHRH) have demonstrated the presence of LHRH-like immunoreactive peptides in a wide range of vertebrates. Contrary to previous reports, the molecule differs in various vertebrates. Avian, reptilian, and teleostean LHRH's are chemically distinct from the mammalian peptide but are in themselves indistinguishable. However, amphibian LHRH appears to be identical to the mammalian peptide. These findings have interesting evolutionary implications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, J A -- Millar, R P -- New York, N.Y. -- Science. 1979 Oct 5;206(4414):67-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/384514" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Chromatography ; Gonadotropin-Releasing Hormone/*analysis/immunology ; Hypothalamus/analysis ; Radioimmunoassay ; Species Specificity ; 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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  • 4
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    Fibrinopeptide B and aggregation of fibrinogen (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-04-13
    Description: Removal of fibrinopeptide B from human fibrinogen by reaction with the procoagulant enzyme from copperhead snake venom below 25 degrees C resulted in tight aggregation of the fibrinogen, which, in turn, progressively blocked a concomitant but sluggish release of fibrinopeptide A by the enzyme. When the clots obtained at less than 25 degrees C were warmed, they dissociated into soluble aggregates and monomers. Release of fibrinopeptide A then resumed, and a secondary coagulation followed. The aggregation induced by release of fibrinopeptide B itself involves a plasmin-susceptible segment located just distal to B in the B beta chain of fibrinogen, a segment previously shown to be of little importance in the aggregation induced by release of fibrinopeptide A.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shainoff, J R -- Dardik, B N -- New York, N.Y. -- Science. 1979 Apr 13;204(4389):200-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/155308" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crotalid Venoms/*metabolism ; Fibrinogen/*metabolism ; Fibrinolysin/metabolism ; Fibrinopeptide A/metabolism ; Fibrinopeptide B/*metabolism ; Humans ; Molecular Weight ; Protein Binding ; Temperature
    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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    Evolutionary relatedness of viper and primate endogenous retroviruses (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-04-20
    Description: A retrovirus previously isolated from a tumored Russell's viper is shown by molecular hybridization to be an endogenous virus of this reptilian species. Radio-immunologic techniques revealed that the viper retrovirus is immunologically and, hence, evolutionarily related to endogenous type D retorviruses of Old World primates. These findings extend the number of vertebrate classes possessing endogenous retroviruses and suggest that type D retroviruses may even be more widely distributed in nature than type C retroviruses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Andersen, P R -- Barbacid, M -- Tronick, S R -- Clark, H F -- Aaronson, S A -- New York, N.Y. -- Science. 1979 Apr 20;204(4390):318-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/219480" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Viral/analysis ; Base Sequence ; *Biological Evolution ; *Genes, Viral ; Nucleic Acid Hybridization ; Primates/*microbiology ; Retroviridae/*genetics/immunology ; Snakes/genetics/*microbiology ; Viral Proteins/immunology
    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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    Space-filling models of kinase clefts and conformation changes (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-04-27
    Description: Space-filling models of yeast hexokinase, adenylate kinase, and phosphoglycerate kinase drawn by computer clearly portray the bilobal character of these phosphoryl transfer enzymes, and the deep cleft which is formed between the lobes. A dramatic conformational change occurs in hexokinase as glucose binds to the bottom of the cleft, which causes the two lobes of hexokinase to come together. A substrate-induced closing of the active site cleft is postulated to occur in other kinases as well. This change may provide a mechanism by which some of these enzymes reduce their inherent adenosine triphosphatase activity and could be a general requirement of the kinase reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, C M -- Zucker, F H -- Steitz, T A -- New York, N.Y. -- Science. 1979 Apr 27;204(4391):375-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/220706" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylate Kinase ; Binding Sites ; Catalysis ; Hexokinase ; Models, Molecular ; Phosphoglycerate Kinase ; *Phosphotransferases ; Protein Conformation ; Saccharomyces cerevisiae/enzymology ; 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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  • 7
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    Tumor surveillance: how tumors may resist macrophage-mediated host defense (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-01-12
    Description: Both normal human serum and supernatant from explanted malignant tumors contained a heat-stable low-molecular-weight factor that inhibited monocyte activation in vitro. In contrast, serum from individuals with solid tumors enhanced monocyte activation. It is suggested that the systemic activation of monocytes that occurs in malignant disease may be an appropriate host response but that successful tumors may continue to grow because they subvert the normal physiological signal for inhibition of macrophage activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rhodes, J -- Bishop, M -- Benfield, J -- New York, N.Y. -- Science. 1979 Jan 12;203(4376):179-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/758686" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Carcinoma/*immunology ; Carcinoma, Squamous Cell/immunology ; Chemotaxis ; Colonic Neoplasms/*immunology ; Humans ; Immunity, Cellular ; Immunoglobulin Fc Fragments ; Lung Neoplasms/*immunology ; Macrophages/*immunology ; Monocytes/*immunology ; Rosette Formation
    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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    Endothermy and activity in vertebrates (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-11-09
    Description: Resting and maximal levels of oxygen consumption of endothermic vertebrates exceed those of ectotherms by an average of five- to tenfold. Endotherms have a much broader range of activity that can be sustained by this augmented aerobic metabolism. Ectotherms are more reliant upon, and limited by, anaerobic metabolism during activity. A principal factor in the evolution of endothermy was the increase in aerobic capacities to support sustained activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bennett, A F -- Ruben, J A -- New York, N.Y. -- Science. 1979 Nov 9;206(4419):649-54.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/493968" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Adenosine Triphosphate/biosynthesis ; Animals ; *Biological Evolution ; *Body Temperature Regulation ; *Energy Metabolism ; Locomotion ; Motor Activity ; Oxygen Consumption ; Selection, Genetic ; Vertebrates/*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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  • 9
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    Acridine araphanes: a new class of probe molecules for biological systems (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    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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    The major histocompatibility complex of the mouse (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-02-09
    Description: Like physicists striving to develop a unified field theory, immunologists are attempting to bring order to the microcosmos of defense reactions. Indications are that one of the most important constants in this microcosmos is the major histocompatibility complex (MHC) of the species. A test of any interpretation of the MHC's role in immunity is how well it explains this system's polymorphism. One of the most crucial questions an MHC hypothesis must answer is: Why are there so many alleles at this complex?〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klein, J -- New York, N.Y. -- Science. 1979 Feb 9;203(4380):516-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/104386" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Blood Proteins/genetics ; Genes ; *Genes, MHC Class II ; Genetic Linkage ; H-2 Antigens/*genetics ; Lymphocytes/immunology ; *Major Histocompatibility Complex ; Mice/*immunology ; Phenotype ; Polymorphism, Genetic
    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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  • 11
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    Embryonic rodent brain contains estrogen receptors (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-05-04
    Description: Estradiol-binding proteins with the properties of putative estrogen receptors are present in cytosol extracts of embryonic mouse hypothalamus and other brain regions. These embryonic estrogen receptors are adultlike in their high affinity and limited capacity for estradiol, sensitivity to diethylstilbestrol, ability to adhere to DNA, and behavior during DNA-cellulose affinity chromatography. As early as 4 days before birth, mouse hypothalamus has approximately 40 percent of the adult concentration of hypothalamic estrogen receptors with these properties. These observations raise the possibility that embryonic rodent brain has the biochemical potential to respond to sex hormones and that the critical period of brain sexual differentiation could be initiated prenatally.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vito, C C -- Fox, T O -- New York, N.Y. -- Science. 1979 May 4;204(4392):517-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/432656" target="_blank"〉PubMed〈/a〉
    Keywords: Age Factors ; Animals ; Binding Sites ; Brain/*embryology ; Chromatography, Affinity ; Cytosol/metabolism ; Hypothalamus/embryology ; Mice ; Receptors, Estrogen/*metabolism ; Sexual Maturation
    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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