Fractionation of CNBr fragments and primary structures of peptides of the adenovirus hexon protein.
The adenovirus hexon protein has been carboxymethylated with 14C-labeled iodoacetate. After treatment with CNBr, the peptide mixture was fractionated into fragments with seven size classes by exclusion chromatography. Large fragments were further purified by CM-cellulose chromatography in urea, and small fragments were purified by high voltage paper electrophoresis. Amino acid sequences of pure fragments have been determined by combined use of sequenator-based direct degradations, and of manual t-dimethylaminonaphthalene-1-sulfonyl-monitored Edman degradations subsequent to enzymatic redigestions. Fractionations are given, the primary structures of 22 CNBr fragments containing a total of 677 residues are reported, and the analytical aspects of the structural properties are considered.
D000260:Adenoviruses, Human / Q000032:analysis*; D000595:Amino Acid Sequence; D002213:Capsid; D036022:Capsid Proteins; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003488:Cyanogen Bromide; D004590:Electrophoresis, Paper; D007461:Iodoacetates; D010446:Peptide Fragments / Q000302:isolation & purification*; D014764:Viral Proteins
D036022:Capsid Proteins; D007461:Iodoacetates; D010446:Peptide Fragments; D014764:Viral Proteins; C018315:hexon capsid protein, Adenovirus; D003488:Cyanogen Bromide