Amphiphilic properties of the avian myeloblastosis virus major glycoprotein, gp 80

✍ Scribed by Dante J. Marciani

• Book ID: 102877557
• Publisher: John Wiley and Sons
• Year: 1983
• Tongue: English
• Weight: 693 KB
• Volume: 22
• Category: Article
• ISSN: 0730-2312
• DOI: 10.1002/jcb.240220403

✦ Synopsis

The major glycoprotein (gp 80) from avian myeloblastosis virus (AMV) displays significant lipophilic properties, as shown by its strong interactions with acetylated uncharged decylamino agarose in hydrophobic chromatography. In effect, release from binding was achieved only by the added presence of a polarity reducing agent (ethylene glycol) and the strong anionic detergent sodium dodecyl sulfate. The hydrophobic behavior of the glycoprotein, coupled to the high content of hydrophilic carbohydrates, indicates its amphiphilic character. Confirmation of the amphiphilic nature of the A M V gp 80 was obtained by charge shift electrophoresis and crossed hydrophobic interaction immunoelectrophoresis. In both instances, the electrophoretic behavior of the glycoprotein was dependent on the presence of detergents. The A M V gp 80 displays the properties of integral membrane proteins.