Structural proteins of murine erythroblastosis virus

✍ Scribed by L. V. McDugald; S. Panem; W. H. Kirsten

• Book ID: 102863380
• Publisher: John Wiley and Sons
• Year: 1970
• Tongue: French
• Weight: 511 KB
• Volume: 5
• Category: Article
• ISSN: 0020-7136
• DOI: 10.1002/ijc.2910050109

✦ Synopsis

Abstract

^3^H‐amino‐acid labelled murine erythroblastosis virus (MEV) was harvested from the EMS cell line and purified by centrifugation in sucrose or potassium‐citrate gradients. ^3^H‐amino‐acid labelled nucleoids were isolated from MEV by the tween‐ether method. Proteins were solubilized from whole MEV and MEV‐nucleoids. Electrophoresis in polyacrylamide gels of pH 7.2 in 0.5 M urea for 17 h yielded three major peaks of radioactivity from whole MEV preparations. These proteins were referred to as MEV‐1, MEV‐2 and MEV‐3. In addition, two minor protein peaks, MEV‐a and MEV‐b, were recovered from whole MEV. Only two major peaks, MEV‐1 and MEV‐2, and one minor component, MEV‐a, were found in electropherograms of MEV‐nucleoids. The results were reproducible with MEV progeny harvested from later subcultures of EMS cells. The results suggested that MEV‐3 and MEV‐b were structural proteins of either the virion coat or the internal virion structure.