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  • T4 bacteriophage  (1)
  • adhesion  (1)
  • Wiley-Blackwell  (2)
  • American Association for the Advancement of Science
  • 1980-1984  (2)
  • 1965-1969
Collection
Publisher
  • Wiley-Blackwell  (2)
  • American Association for the Advancement of Science
Years
  • 1980-1984  (2)
  • 1965-1969
Year
  • 1
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 18 (1982), S. 363-375 
    ISSN: 0730-2312
    Keywords: T4 bacteriophage ; short-tail fibers ; fiber formation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The characteristics of pure preparations of short-tail fibers of bacteriophage T4 have been studied in the optical and electron microscope. Three main structures were observed: 1) spheres of 8.1 nm diameter; 2) fibers 43 nm long and 3.8 nm thick; and 3) fibers 54 nm long and 3.2 nm thick. Both types of fibers exhibited a regular beaded appearance. The 43-nm fibers were the most abundant structure. During the process of purification of the short-tail fibers, the formation of aggregates was observed each time the material containing the short-tail fibers was dialyzed against saline solutions. These aggregates became increasingly fibrous (as observed in the optical microscope) as the material used was increasingly enriched in short-tail fibers. Finally, most of the aggregates were of the fibrous type when they were formed from a purified preparation of short-tail fibers. In the electron microscope, it was found that the filamentous aggregates were organized in well-defined bundles. The amino acid composition of the highly purified short-tail fibers was also determined. Among the known fibrous proteins, the ones that most resemble the amino acid composition of the short-tail fibers are actin and fibrinogen. These observations are discussed in relation to the T4 short-tail fiber structure and their localization on the hexagonal baseplate of the T4 tail structure.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 25 (1984), S. 109-121 
    ISSN: 0730-2312
    Keywords: adhesion ; cell surface glycoprotein ; monoclonal antibodies ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Two monoclonal antibodies that cause changes in the morphology of cultured chick myogenic cells have been described previously [8]. In this paper, these antibodies are shown to interact with the same 140Kd protein. The 140Kd protein has been further characterized as a cell-surface glycoprotein by lactoperoxidase-catalyzed iodinations and lectin affinity chromatography. The protein is resistant to digestion by trypsin and collagenase and has been shown to be unrelated to fibronectin by immunoprecipitation studies and by peptide mapping. A second protein, of approximately 170Kd MW; is also immunoprecipitated by the monoclonal antibodies. This protein is probably unrelated to the 140Kd protein since the peptide maps are quite distinct.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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