Title: A Golgi retention signal in a membrane-spanning domain of coronavirus E1 protein Document date: 1991_10_1
ID: s4a8zs5a_22
Snippet: Oligomerization of the Gml protein was analyzed by velocity gradient centrifugation in sucrose essentially as described (7) . Continuous 5 to 20% sucrose gradients were poured over a 0.25 ml 60% sucrose cushion in SW50.1 tubes . All solutions were in 20 mM Tris, 30 mM MES, pH 5 .8, 1% Triton X-100, 100 mM NaCl . HeLa cells expressing either G or Gml were labeled with [35 S]cysteine for 10 min and harvested immediately or after 20 min of chase in .....
Document: Oligomerization of the Gml protein was analyzed by velocity gradient centrifugation in sucrose essentially as described (7) . Continuous 5 to 20% sucrose gradients were poured over a 0.25 ml 60% sucrose cushion in SW50.1 tubes . All solutions were in 20 mM Tris, 30 mM MES, pH 5 .8, 1% Triton X-100, 100 mM NaCl . HeLa cells expressing either G or Gml were labeled with [35 S]cysteine for 10 min and harvested immediately or after 20 min of chase in unlabeled cysteine . Lysates were loaded on top of the gradients and spun at 47,000 rpm for 16 h . Fractions (0.33 ml) were collected, immunoprecipitated with antiVSV antibody, and electrophoresed to determine the location of G protein in the gradient .
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