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  • Species Specificity  (15)
  • Rabbits  (11)
  • American Association for the Advancement of Science (AAAS)  (26)
  • 1980-1984  (26)
  • 1965-1969
  • 1982  (12)
  • 1980  (14)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (26)
Years
  • 1980-1984  (26)
  • 1965-1969
Year
  • 1
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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
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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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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  • 3
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    Antibody to spermine: a natural biological constituent (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-06-06
    Description: A protein that binds spermine specifically was separated from normal rabbit serum by affinity chromatography. Immunoelectrophoresis, the Ouchterlony immunodiffusion test, and gradient gel electrophoresis indicated that this protein has immunoglobulin characteristics and consists of several populations of antibodies to spermine. These were sequentially released from Sepharose-spermine gel by step-wise elution with solutions ranging in pH from 4 to 1. The binding constants varied from 5.0 x 10(8) to 11.1 x 10(8) liters per mole. These globulins did not react with monoacetylputrescine, L-ornithine, L-lysine, and histamine. Negligible cross-reactivity was detected with spermidine, putrescine, N8-monoacetylspermidine, cadaverine, and diaminopropane. Since perturbations in polyamine metabolism have been identified in several diseases, the study of extracellular polyamine homeostasis may reveal an important regulatory function for this protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bartos, D -- Bartos, F -- Campbell, R A -- Grettie, D P -- Smejtek, P -- New York, N.Y. -- Science. 1980 Jun 6;208(4448):1178-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7375929" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies/*isolation & purification ; Binding Sites, Antibody ; Chromatography, Affinity ; Homeostasis ; Immunoglobulin G/isolation & purification ; Kinetics ; Rabbits ; Spermine/*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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  • 4
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    Differential breakdown of phylogenetically diverse ribosomal RNA's inserted via liposomes into mammalian cells (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-07-02
    Description: Liposomes were used to deliver ribosomal RNA's from the different organisms into cultivated mouse plasmacytoma cells. Ribosomal RNA from Escherichia coli was degraded intracellularly within 1 hour, whereas mouse and yeast ribosomal RNA's were degraded more slowly. This indicates that cells can discriminated between different ribosomal RNA's.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lavelle, D -- Ostro, M J -- Giacomoni, D -- GM 27935/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1982 Jul 2;217(4554):59-61.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6178157" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Escherichia coli ; Kinetics ; *Liposomes ; Mice ; Molecular Weight ; Neoplasms, Experimental/metabolism ; Plasmacytoma/*metabolism ; RNA, Bacterial/metabolism ; RNA, Ribosomal/*metabolism ; Saccharomyces cerevisiae ; Species 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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  • 5
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    Rotational invariance in visual pattern recognition by pigeons and humans (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-11-19
    Description: Pigeons and humans chose which one of two alternative visual forms was identical to, or a mirror image of, a previously presented sample form. The two comparison forms were presented in various orientations with respect to the sample. The two species yielded similar accuracies, but although human reaction times depended linearly on the angular disparities, those of the pigeon did not. Humans appeared to apply a well-known, thoughtlike, mental rotation procedure to the problem, whereas pigeons seemed to rely on a more efficient automatic process that humans can use only in simpler rotational invariance tasks. Mirror-image forms may be better discriminated by the pigeon's visual system than by the human one.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hollard, V D -- Delius, J D -- New York, N.Y. -- Science. 1982 Nov 19;218(4574):804-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7134976" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Columbidae ; Discrimination (Psychology) ; Humans ; Rotation ; Species Specificity ; *Visual Perception
    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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    The phylogeny of prokaryotes (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-07-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fox, G E -- Stackebrandt, E -- Hespell, R B -- Gibson, J -- Maniloff, J -- Dyer, T A -- Wolfe, R S -- Balch, W E -- Tanner, R S -- Magrum, L J -- Zablen, L B -- Blakemore, R -- Gupta, R -- Bonen, L -- Lewis, B J -- Stahl, D A -- Luehrsen, K R -- Chen, K N -- Woese, C R -- New York, N.Y. -- Science. 1980 Jul 25;209(4455):457-63.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6771870" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteria/*classification ; Base Sequence ; Biological Evolution ; Chloroplasts/analysis ; Clostridium/classification ; Cyanobacteria/classification ; DNA/analysis ; *Phylogeny ; RNA, Ribosomal/*analysis ; Species Specificity
    Print ISSN: 0036-8075
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  • 7
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    Insertion of a new gene of viral origin into bone marrow cells of mice (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-05-30
    Description: DNA containing the herpes simplex virus thymidine kinase (HSVtk) gene was used to transform wild-type tk+ mouse L cells to a tk++ status in vitro using methotrexate as a selective agent. HSVtk DNA was also used to transform mouse bone marrow cells in vitro. Transformed marrow cells injected into irradiated and methotrexate-treated recipient mice gave rise to proliferating cells which in some cases dominated the marrow population and which contained HSVtk gene sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mercola, K E -- Stang, H D -- Browne, J -- Salser, W -- Cline, M J -- New York, N.Y. -- Science. 1980 May 30;208(4447):1033-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6246577" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone Marrow/*enzymology ; Bone Marrow Transplantation ; DNA, Viral/analysis ; Drug Resistance ; *Genes, Viral ; L Cells (Cell Line) ; Methotrexate/pharmacology ; Mice ; Simplexvirus/enzymology/*genetics ; Species Specificity ; Thymidine Kinase/*genetics ; *Transformation, Genetic
    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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  • 8
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    Evolutionary conservation of repetitive sequence expression in sea urchin egg RNA's (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-05-30
    Description: Cloned repetitive DNA sequences were used to determine the number of homologous RNA transcripts in the eggs of two sea urchin species, Strongylocentrotus purpuratus and S. franciscanus. The eggs of these species contain different amounts of RNA, and their genomes contain different numbers of copies of the cloned repeats. The specific pattern of repetitive sequence representation in the two egg RNA's is nonetheless quantitatively similar. The evolutionary conservation of this pattern suggests the functional importance of repeat sequence expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moore, G P -- Costantini, F D -- Posakony, J W -- Davidson, E H -- Britten, R J -- New York, N.Y. -- Science. 1980 May 30;208(4447):1046-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6154974" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Biological Evolution ; DNA, Recombinant ; Female ; Nucleic Acid Hybridization ; Ovum/physiology ; Plasmids ; RNA/*genetics ; Sea Urchins/*genetics ; Species Specificity ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 9
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    Bladder-surface glycosaminoglycans: an efficient mechanism of environmental adaptation (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-05-09
    Description: The transitional epithelium of the urinary bladder secretes and binds to its surface a glycosaminoglycan than inhibits the adherence of bacteria. Synthetic sulfonated glycosaminoglycans instilled intraluminally into bladders whose natural mucin layer has been removed are as effective as the natural mucin in preventing bacterial adherence. It also appears that adherence of calcium and protein is reduced in the presence of both the natural mucin layer and the synthetic sulfonated glycosaminoglycan sodium pentosanpolysulfate, suggesting that the antiadherence activity of both natural and synthetic surface glycosaminoglycans in the bladder extends to the molecular and ionic levels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parsons, C L -- Stauffer, C -- Schmidt, J D -- New York, N.Y. -- Science. 1980 May 9;208(4444):605-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6154316" target="_blank"〉PubMed〈/a〉
    Keywords: Adsorption ; Animals ; Calcium/metabolism ; Cell Adhesion ; Environmental Exposure ; Epithelium/physiology ; Glycosaminoglycans/*physiology ; Male ; Mucins/pharmacology ; Pentosan Sulfuric Polyester/pharmacology ; Protein Binding/drug effects ; Proteins/metabolism ; Rabbits ; Urinary Bladder/microbiology/*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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  • 10
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    Sperm-egg interaction: evidence for boar sperm plasma membrane receptors for porcine zona pellucida (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-01-04
    Description: Freshly ejaculated, noncapacitated boar sperm bind rapidly and in large numbers to pig egg zona pellucida in vitro. In the present study, the number of sperm bound decreased sharply when sperm motility was lowered by energy poisons or by reducing the temperature. Highly motile sperm from humans, guinea pigs, and rats, added at concentrations ten times higher than control sperm, did not bind to the porcine zona. At the same high concentration, a small number of hamster and bull sperm bound to the zona. Binding of boar sperm to the zona pellucida was blocked almost completely by diluted whole antiserum to sperm plasma membranes and by univalent (Fab) antibody to these membranes. When antibody to sperm plasma membrane was first absorbed with plasma membrane vesicles, sperm binding was not inhibited. These results provide direct evidence for the existence of sperm plasma membrane receptors for the zona pellucida of the pig.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peterson, R N -- Russell, L -- Bundman, D -- Freund, M -- New York, N.Y. -- Science. 1980 Jan 4;207(4426):73-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7188647" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Cell Membrane/metabolism ; Female ; *Fertilization ; Guinea Pigs ; Humans ; Immunoglobulin Fab Fragments ; Male ; Ovum/*metabolism ; Rats ; Receptors, Drug/metabolism ; Species Specificity ; *Sperm-Ovum Interactions ; Spermatozoa/*metabolism ; Swine ; Zona Pellucida/*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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