Title: A Golgi retention signal in a membrane-spanning domain of coronavirus E1 protein Document date: 1991_10_1
ID: s4a8zs5a_21
Snippet: For G proteins, the kinetics of oligosaccharide processing were determined in cells labeled for 10 min followed by various chase times . Immunoprecipitates were treated with endo H (0.1 mU) as described (28) . Fluorograms were quantitated by densitometry. Trfmer Assay Figure 3 . Gml forms an oligomer larger than a trimer. HeLa cells expressing either G or Gml were labeled for 10 min, and lysed immediately or after a 20 min chase in unlabeled cyst.....
Document: For G proteins, the kinetics of oligosaccharide processing were determined in cells labeled for 10 min followed by various chase times . Immunoprecipitates were treated with endo H (0.1 mU) as described (28) . Fluorograms were quantitated by densitometry. Trfmer Assay Figure 3 . Gml forms an oligomer larger than a trimer. HeLa cells expressing either G or Gml were labeled for 10 min, and lysed immediately or after a 20 min chase in unlabeled cysteine . Lysates were centrifuged in 5 to 20 % continuous sucrose gradients, and gradient fractions were immunoprecipitated with antiVSV serum (see Materials and Methods) . A portion (20%) of each cell lysate was immunoprecipitated directly, and run in the far right-hand lane of each gel . Although apparently a monomer after synthesis, Gml formed a large (>15S) aggregate during the chase .
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