| pubmed-article:3014781 | pubmed:abstractText | Proteins from bovine leukemia virus (BLV) were investigated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis in the presence and absence of 14C amino acids. Virus grown either in fetal lamb kidney (FLK) or bat lung (BL) cells revealed seven major proteins designated p10, p12, p15(1), p15(2), p24, gp30, and gp64. By tryptic peptide analysis, N-terminal amino acid analysis and radioimmunoassay it could be shown that p10, a basic protein with hydrophobic properties, is a cleavage product of p15(2), the acidic and slightly hydrophobic phosphoprotein of BLV. The structural protein p12 was shown to be a phosphorylated protein identifying it as a second major viral protein to contain phosphorous. Investigation of [3H]glucosamine incorporation, N-terminal amino acid analysis and hydrophobic properties by chloroform-methanol extraction confirmed properties of gp30 and gp64 predicted by nucleotide sequence data. The two p15 proteins have been characterized in more detail. | lld:pubmed |
