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Institute of Virology, University of Vienna, Vienna, Austria
Treatment of tick-borne encephalitis (TBE) virus with Triton X-100 (TX-100), octylglucoside (OG) or cetyltrimethylammonium bromide (CTAB) caused dissociation of the virus envelope into dimers or monomers of the glycoprotein V3. By centrifugation into detergent-free sucrose density gradients, these subunits were found to reassociate and to form haemagglutinating homogeneous glycoprotein complexes sedimenting at 15 to 16, 16 to 18 and 11 to 12S after TX-100, OG and CTAB treatment, respectively. Glycoprotein complexes obtained after TX-100 solubilization contained less than 1% lipid and detergent by weight.
Received 31 October 1979;
accepted 15 February 1980.
This article has been cited by other articles:
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K. Stiasny, S. L. Allison, C. W. Mandl, and F. X. Heinz Role of Metastability and Acidic pH in Membrane Fusion by Tick-Borne Encephalitis Virus J. Virol., August 15, 2001; 75(16): 7392 - 7398. [Abstract] [Full Text] [PDF] |
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