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  • Cattle  (6)
  • American Association for the Advancement of Science (AAAS)  (6)
  • Periodicals Archive Online (PAO)
  • 1980-1984  (6)
  • 1955-1959
  • 1940-1944
  • 1981  (6)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (6)
  • Periodicals Archive Online (PAO)
Years
  • 1980-1984  (6)
  • 1955-1959
  • 1940-1944
Year
  • 1
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    Cloned viral protein vaccine for foot-and-mouth disease: responses in cattle and swine (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-12-04
    Description: A DNA sequence coding for the immunogenic capsid protein VP3 of foot-and-mouth disease virus A12, prepared from the virion RNA, was ligated to a plasmid designed to express a chimeric protein from the Escherichia coli tryptophan promoter-operator system. When Escherichia coli transformed with this plasmid was grown in tryptophan-depleted media, approximately 17 percent of the total cellular protein was found to be an insoluble and stable chimeric protein. The purified chimeric protein competed equally on a molar basis with VP3 for specific antibodies to foot-and-mouth disease virus. When inoculated into six cattle and two swine, this protein elicited high levels of neutralizing antibody and protection against challenge with foot-and-mouth disease virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kleid, D G -- Yansura, D -- Small, B -- Dowbenko, D -- Moore, D M -- Grubman, M J -- McKercher, P D -- Morgan, D O -- Robertson, B H -- Bachrach, H L -- New York, N.Y. -- Science. 1981 Dec 4;214(4525):1125-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6272395" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibody Formation ; Base Sequence ; Cattle ; Cattle Diseases/*prevention & control ; *Cloning, Molecular ; DNA Restriction Enzymes ; DNA, Recombinant/metabolism ; Foot-and-Mouth Disease/*prevention & control ; Immunity, Cellular ; Protein Biosynthesis ; Swine ; Swine Diseases/*prevention & control ; Transcription, Genetic ; *Vaccines ; Viral Proteins/genetics/*therapeutic use
    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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    Phosphorus distribution in the nucleosome (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-01-09
    Description: The spatial distribution of phosphorus within active fraction nucleosomes reveals that the path of the DNA is consistent with one and three-fourths turns of DNA supercoiled around the outside of the protein core. This phosphorus distribution, obtained with an imaging electron spectrometer in a conventional transmission electron microscope, simultaneously establishes new limits of sensitivity for elemental microanalysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bazett-Jones, D P -- Ottensmeyer, F P -- New York, N.Y. -- Science. 1981 Jan 9;211(4478):169-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7444457" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Dna ; Electron Probe Microanalysis ; Microscopy, Electron/methods ; Nucleic Acid Conformation ; Nucleosomes/*ultrastructure ; *Phosphorus ; Transcription, Genetic
    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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  • 3
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    Bovine babesiosis: protection of cattle with culture-derived soluble Babesia bovis antigen (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-04-17
    Description: Adult Hereford (Bos taurus) cattle were protected from severe reactions and death caused by the tick-borne protozoan hemoparasite Babesia bovis, 3 months after vaccination with a cell culture--derived immunogen. The immunogen consisted of filtered, freeze-dried supernatant fluid collected from long-term cultures of Babesia bovis in vitro. It was reconstituted with saponin adjuvant and injected twice subcutaneously at 2-week intervals. Serum collected from vaccinated cattle caused thickening of the merozoite surface coat, aggregation, and lysis of merozoites in vitro. This reaction was identical to that caused by serum from immune carrier cattle suggesting that the protective antigen present in culture fluids is merozoite surface coat antigen. No mortality occurred among vaccinated cattle, whereas mortality among unvaccinated cattle and Babesia bigemina--immune cattle was 62.5 percent indicating that immunity to bovine babesiosis is species-specific.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, R D -- James, M A -- Ristic, M -- Aikawa, M -- Vega y Murguia, C A -- AI 16680/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1981 Apr 17;212(4492):335-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7209532" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens/*administration & dosage ; Babesia/immunology/ultrastructure ; Babesiosis/*prevention & control ; Cattle ; Cattle Diseases/*prevention & control ; Culture Media ; *Vaccination
    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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  • 4
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    Morphine in cow and human milk: could dietary morphine constitute a ligand for specific morphine (mu) receptors? (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-08-28
    Description: Morphine has been found in cow and human milk at concentrations of 200 to 500 nanograms per liter. Multistep purification yields a material that has immunological, biological, pharmacological, and chemical properties identical to those of morphine. Similar morphine-like material, which has been tentatively identified in some common plant sources, may be a ubiquitous dietary constituent and a possible source for the material in milk. Since morphine (mu) receptors have a low affinity for enkephalins, and since morphine-like materials have been described in brain and intestine, it is possible that morphine in food may be the source of this material and a normal ligand specific for mu receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hazum, E -- Sabatka, J J -- Chang, K J -- Brent, D A -- Findlay, J W -- Cuatrecasas, P -- New York, N.Y. -- Science. 1981 Aug 28;213(4511):1010-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6267691" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Diet ; Female ; Humans ; Ligands ; Milk/*analysis ; Milk, Human/analysis ; Morphine/*analysis/metabolism ; Receptors, Opioid/*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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  • 5
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    Fc and C3b receptors on pulmonary endothelial cells: induction by injury (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-10-30
    Description: Receptors for the activated third component of complement and for the Fc portion of immunoglobulin G are not expressed by apparently normal bovine pulmonary endothelial cells, but are expressed when the cells are exposed to white cell lysates or are infected with influenza or cytomegalovirus. The unmasking of these latent receptors may contribute to the pulmonary inflammatory response characteristic of, for example, anaphylaxis and to those lung diseases characterized by the deposition of immune complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ryan, U S -- Schultz, D R -- Ruan, J W -- HL 21568/HL/NHLBI NIH HHS/ -- HL 22087/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1981 Oct 30;214(4520):557-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6270789" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Cells, Cultured ; Complement C3b/metabolism ; Cytomegalovirus Infections/physiopathology ; Endothelium/metabolism ; Orthomyxoviridae Infections/physiopathology ; Pulmonary Artery/*cytology ; Receptors, Complement/*metabolism ; Receptors, Fc/*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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  • 6
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    Species restriction of a monoclonal antibody reacting with residues 130 to 137 in encephalitogenic myelin basic protein (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-10-02
    Description: A monoclonal antibody (immunoglobulin G1) has been produced that reacts against myelin basic protein present in or extracted from the brains of many mammals-with certain important exceptions. Because of known species differences in amino acid sequences of basic protein and of certain peptide fragments, the binding site for this particular antibody appeared likely to include residues 130 to 137. Confirmation of this hypothesis was obtained by amino acid composition of the major immunoreactive peptides produced by thermolysin digestion of human basic protein and isolated by high-performance liquid chromatography.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sires, L R -- Hruby, S -- Alvord, E C Jr -- Hellstrom, I -- Hellstrom, K E -- Kies, M W -- Martemspm, R -- Deibler, G E -- Beckman, E D -- Casnellie, J E -- CA-19148/CA/NCI NIH HHS/ -- CA-25558/CA/NCI NIH HHS/ -- CA-26584/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1981 Oct 2;214(4516):87-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6169147" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Cattle ; Chickens ; Epitopes ; Guinea Pigs ; Humans ; Macaca ; Myelin Basic Protein/*immunology ; Peptide Fragments/immunology ; Rabbits ; Rats ; Species Specificity
    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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