Proteins of Kirsten murine leukaemia-sarcoma virus: localization within the virus particle by iodination and fractionation techniques.
The protein and glycoprotein composition of Kirsten murine leukaemia-sarcoma virus (KiMSV(KiMuLV) was studied using SDS-polyacrylamide gel electrophoresis. Twenty-three polypeptides and three glycoproteins were detected following electrophoresis by staining with Coomassie blue and PAS or by autoradiography of isotopically labelled virus. Protein components were assigned positions in the virus particle, envelope, nucleoid or intermediate area based on  iodination with lactoperoxidase and sedimentation in potassium citrate equilibrium gradients. The KiMSV (KiMuLV) envelope contained 11 polypeptides and three glycoproteins. The  virus nucleoid and intermediate area were each composed of six proteins. The protein composition of KiMSV(KiMuLV) was highly  reproducible when virus was harvested from cells of the same subcluture generation. However, the protein profiles were altered with repeated in vitro passages of the virus-producing cell line.
D001345:Autoradiography; D002250:Carbon Radioisotopes; D005591:Chemical Fractionation; D003902:Detergents; D004591:Electrophoresis, Polyacrylamide Gel; D017988:Gammaretrovirus / Q000032:analysis*; D006023:Glycoproteins / Q000032:analysis; D007457:Iodine Radioisotopes; D011492:Protein Hydrolysates; D012967:Sodium Dodecyl Sulfate; D014764:Viral Proteins / Q000032:analysis*
D002250:Carbon Radioisotopes; D003902:Detergents; D006023:Glycoproteins; D007457:Iodine Radioisotopes; D011492:Protein Hydrolysates; D014764:Viral Proteins; D012967:Sodium Dodecyl Sulfate