Jörnvall H, von Bahr-Lindström H
J Biol Chem. 1981 Jun 25;256(12):6187-98.
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.
腺病毒六邻体蛋白已用14C标记的碘乙酸进行了羧甲基化。用溴化氰处理后,通过排阻色谱法将肽混合物分离成七个大小类别的片段。大片段在尿素中通过CM-纤维素色谱法进一步纯化,小片段通过高压纸电泳纯化。通过基于序列分析仪的直接降解以及酶解后手动进行的t-二甲基氨基萘-1-磺酰基监测的埃德曼降解相结合的方法,确定了纯片段的氨基酸序列。给出了分级分离情况,报道了22个溴化氰片段的一级结构,共含677个残基,并对结构性质的分析方面进行了探讨。