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Proteins of Kirsten Murine Leukaemia-sarcoma Virus: localization within the Virus Particle by Iodination and Fractionation Techniques

Department of Pathology, Pritzker School of Medicine, Division of Biological Sciences, University of Chicago, Chicago, Illinois 60637, U.S.A.

W. H. Kirsten

Departments of Pathology and Pediatrics, Pritzker School of Medicine, Division of Biological Sciences and Joseph P. Kennedy, Jun. Mental Retardation Center, University of Chicago, Chicago, Illinois 60637, U.S.A.

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 subculture generation. However, the protein profiles were altered with repeated in vitro passages of the virus-producing cell line.

Received 30 May 1974; accepted 30 August 1974.

This article has been cited by other articles:

				S Panem, E. Prochownik, F. Reale, and W. Kirsten Isolation of type C virions from a normal human fibroblast strain Science, July 25, 1975; 189(4199): 297 - 299. [Abstract] [PDF]