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Fractionation of CNBr fragments and primary structures of peptides of the adenovirus hexon protein.

Authors
  • Jörnvall, H
  • von Bahr-Lindström, H
Type
Published Article
Journal
Journal of Biological Chemistry
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Publication Date
Jun 25, 1981
Volume
256
Issue
12
Pages
6187–6198
Identifiers
PMID: 7240197
Source
Medline
License
Unknown

Abstract

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.

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