• 1 January 1982
    • journal article
    • research article
    • Vol. 29  (4) , 369-375
Abstract
The protein composition of type-D oncovirus HEp-2, isolated from cell-free medium of continuous human [laryngeal carcinoma] HEp-2 cell line, was investigated using electrophoresis on gradient polyacrylamide gels with sodium dodecyl sulfate (SDS). Labeling with 14C-amino acids revealed 5 viral polypeptides with MW of 70,000 (gp70), 27,000 (p27), 19,000 (p19), 15,000 (p15), 12,000-10,000 (p12-10). The 70,000 dalton protein was shown to be the only glycoprotein by incorporation of radioactive glucosamine. A polypeptide with MW of 78,000 was specifically precipitated from pulse-labeled type-D oncovirus producing HEp-2 cells with goat anti Mason-Pfizer p27 serum. This protein was gag gene-coded polyprotein precursor (Pr78gag) of the major virus polypeptide p27. Pulse-labeled Hep-2 and Mason-Pfizer infected [human ovarian carcinoma] Tu 197 cells were rinsed, lysed, clarified and precipitated with goat anti Mason-Pfizer p27 serum. In both cases Pr78gag was detected.