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  • Cattle  (7)
  • American Association for the Advancement of Science (AAAS)  (7)
  • Springer Nature
  • 2000-2004
  • 1995-1999
  • 1980-1984  (7)
  • 1940-1944
  • 1980  (7)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (7)
  • Springer Nature
  • Springer  (2)
Years
  • 2000-2004
  • 1995-1999
  • 1980-1984  (7)
  • 1940-1944
Year
  • 1
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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
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Inhibition of cell motility by interferon (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-05-02
    Description: Interferon derived from human leukocytes, human fibroblasts, and mouse fibroblasts was found to inhibit the motility of cultured cells. It inhibits the tumor-induced motility of capillary endothelial cells as well as the spontaneous migration of other cell types. The ability of a given preparation of interferon to inhibit the motility of a given cell type is proportional to its antiviral activity in that particular cell type. Antiserum to human leukocyte interferon neutralizes both the motility-inhibitory activity and the antiviral activity of this preparation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brouty-Boye, D -- Zetter, B R -- New York, N.Y. -- Science. 1980 May 2;208(4443):516-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6154315" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antineoplastic Agents ; Antiviral Agents ; Capillaries/cytology ; Cattle ; *Cell Movement ; Cells, Cultured/physiology ; Endothelium/cytology ; Fibroblasts ; Humans ; Interferons/*pharmacology ; Leukocytes/physiology ; Mice ; Neoplasms/pathology
    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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    Ala-Gly- and Val-Asp-[Arg8]-vasopressin: bovine storage forms of arginine vasopressin with natriuretic activity (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-02-22
    Description: Extracts of fresh-frozen bovine neurohypophysis were purified by chromatographic techniques to isolate and characterize the components that produce natriuresis in nondiuretic dogs. Two compounds with natiuretic properties similar to those of synthetic arginine vasopressin accounted for most of the natriuretic activity and appeared to be the prevalent vasopressin-like molecules in the extract. These peptides were Ala-Gly-[Arg8]-vasopressin and Val-Asp-[Arg8]-vasopressin; the natriuretic potency of each appeared to be similar to synthetic arginine vasopressin and could be observed with doses in the range of 50 picomoles. In the dog the most conspicuous difference between synthetic arginine vasopressin and the new vasopressin peptides was the smaller pressor responses to natriuretic doses of the new compounds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gitelman, H J -- Klapper, D G -- Alderman, F R -- Blythe, W B -- New York, N.Y. -- Science. 1980 Feb 22;207(4433):893-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7355269" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arginine Vasopressin/analogs & derivatives/*metabolism/pharmacology ; Biological Assay ; Blood Pressure/drug effects ; Cattle ; Dogs ; Male ; Natriuresis/*drug effects ; Pituitary Gland, Posterior/*metabolism ; Protein Precursors/metabolism ; Structure-Activity Relationship
    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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    1 alpha, 25-Dihydroxyvitamin D3 nuclear receptors in pituitary (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-09-12
    Description: Specific binding of 1 alpha,25-dihydroxyvitamin D(3) was found in nuclear and cytosol fractions of the bovine pituitary. For nuclear binding. the dissociation constant was 0.1 namomole per liter, and maximum binding was 104 femtomoles per milligram of protein. In competition studies, 25-hydroxyvitamin D(3) was 300 times weaker than 1 alpha,25-dihydroxyvitamin D(3). The existence of high-affinity sites supports a physiologic role for 1 alpha,25-dihydroxyvitamin D(3) in the pituitary.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gelbard, H A -- Stern, P H -- U'Prichard, D C -- New York, N.Y. -- Science. 1980 Sep 12;209(4462):1247-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6250221" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/metabolism ; Cattle ; Cell Nucleus/metabolism ; Cholecalciferol/*metabolism ; Cytosol/metabolism ; Dihydroxycholecalciferols/*metabolism ; Hydroxycholecalciferols/*metabolism ; Kinetics ; Pituitary Gland/*metabolism/ultrastructure ; Receptors, Drug/*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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    Relation of mammalian sperm chromatin heterogeneity to fertility (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-12-05
    Description: Flow cytometry of heated sperm nuclei revealed a significant decrease in resistance to in situ denaturation of spermatozoal DNA in samples from bulls, mice, and humans of low or questionable fertility when compared with others of high fertility. Since thermal denaturation of DNA in situ depends on chromatin structure, it is assumed that changes in sperm chromatin conformation may be related to the diminished fertility. Flow cytometry of heated sperm nuclei may provide a new and independent determinant of male fertility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Evenson, D P -- Darzynkiewicz, Z -- Melamed, M R -- New York, N.Y. -- Science. 1980 Dec 5;210(4474):1131-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7444440" target="_blank"〉PubMed〈/a〉
    Keywords: Acridine Orange ; Animals ; Cattle ; Cell Nucleus/ultrastructure ; Chromatin/*ultrastructure ; *Fertility ; Hot Temperature ; Humans ; Infertility, Male/*pathology ; Male ; Mice ; Nucleic Acid Denaturation ; Sperm Head/*ultrastructure ; Spermatozoa/*physiology/*ultrastructure ; Zinc/deficiency
    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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    Cross-linking of lens crystallins in a photodynamic system: a process mediated by singlet oxygen (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-06-13
    Description: In a dye-sensitized photooxidation system, lens crystallin polypeptides become cross-linked, and a blue fluorescence that is associated with the proteins is produced. These changes are similar to those seen in vivo in the aging human lens. Evidence implicating singlet oxygen as the causative agent of the effects in vitro is presented, and the possibility that this species may play a role in aging and cataractogenesis in vivo is discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goosey, J D -- Zigler, J S Jr -- Kinoshita, J H -- New York, N.Y. -- Science. 1980 Jun 13;208(4449):1278-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7375939" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Animals ; Cataract/etiology ; Cattle ; Crystallins/*radiation effects ; Disease Models, Animal ; Fluorescence ; Light ; Methylene Blue ; Oxidation-Reduction ; Oxygen ; Photochemistry ; Riboflavin ; Rose Bengal
    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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    Endothelial cells of bovine pulmonary artery lack receptors for C3b and for the Fc portion of immunoglobulin G (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-05-16
    Description: Bovine pulmonary endothelial cells do not possess receptors for the 3b component of complement (C3b) or for the Fc portion of immunoglobulin G. The lack of these receptors may help explain the nonthrombogenic function of endothelial cells. Our findings rule out the possibility that endothelial cells participate in pulmonary immune complex disease through the binding of C3b or Fc fragments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ryan, U S -- Schultz, D R -- Del Vecchio, P J -- Ryan, J W -- New York, N.Y. -- Science. 1980 May 16;208(4445):748-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7367890" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Cells, Cultured ; Complement C3b/metabolism ; Endothelium/immunology ; Pulmonary Artery/*immunology/metabolism ; Receptors, Complement/*metabolism ; Receptors, Fc/*metabolism ; Rosette Formation
    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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