Purification and characterization of an early glycoprotein from adenovirus type 2-infected cells.
An adenovirus type 2 early glycoprotein with an apparent molecular weight of 19,000 (E19K) in sodium dodecyl sulfate-polyacrylamide gels has been extensively purified. Purification involved detergent solubilization of membrane fractions from infected cells, followed by affinity chromatography on a lectin column and DEAE-Sephadex chromatography. The purified material contained three polypeptides (E40K, E19K, E17.5K), with approximately 90% of the material in the E19K moiety. All three polypeptides yielded identical tryptic peptide maps. The E19K polypeptide contained glucosamine as revealed by [3H]glucosamine labeling of infected cells and amino acid analysis of the purified protein. Immunoprecipitation with a monospecific antiserum showed that the E19K polypeptide started to be synthesized at 2 h, with a maximal rate at 4 h after infection. It was also synthesized at a low rate late in the infectious cycle (12 to 24 h postinfection). Immunoprecipitation from three adenovirus type 2-transformed hamster embryo cell lines and two adenovirus type 2-transformed rat cell lines revealed that one of the hamster cell lines (ad2HE4) and one of the rat cell lines (A2T2C4) expressed this protein.
D000260:Adenoviruses, Human / Q000032:analysis* / Q000378:metabolism; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D006224:Cricetinae; D006023:Glycoproteins / Q000032:analysis / Q000302:isolation & purification*; D006367:HeLa Cells; D008970:Molecular Weight; D010452:Peptide Biosynthesis; D010455:Peptides / Q000032:analysis; D051381:Rats; D014764:Viral Proteins / Q000032:analysis / Q000096:biosynthesis / Q000302:isolation & purification*
D000596:Amino Acids; D006023:Glycoproteins; D010455:Peptides; D014764:Viral Proteins