Premium
Structural proteins of murine erythroblastosis virus
Author(s) -
McDugald L. V.,
Panem S.,
Kirsten W. H.
Publication year - 1970
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910050109
Subject(s) - centrifugation , nucleoid , capsid , amino acid , chemistry , electrophoresis , urea , microbiology and biotechnology , radiochemistry , virus , biology , chromatography , virology , biochemistry , escherichia coli , gene
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.