@article{oai:osaka-aoyama.repo.nii.ac.jp:00000050,
 author = {団野, 源一},
 journal = {大阪青山大学紀要, Journal of Osaka Aoyama University},
 month = {Mar},
 note = {Whole gliadins were separated on a Sephadex G-100 column with 0.1 M acetic acid or 0.01 M aluminum lactate buffer (pH 3.1) as an elution solvent. When a sample of about 95 mg protein was loaded on the column and eluted with 0.1 M acetic acid, the fraction eluted at the void volume of the column was shown to be high molecular weight gliadin by analysis of their electrophoretic patterns on sodium dodecyl sulfate polyacrylamide gel.
The main peak eluted at the near-column volume was low molecular weight gliadins (α－, β－and ω－gliadins, MW about 30,000). A similar elution profile had been reported by Hebner and Wall. In contrast, when 0.01 M aluminum lactate buffer (pH 3.1) was used as an elution solvent, the main peak was eluted at the position of the molecular weight of about 60,000. From these results, we consider that the low molecular weight gliadins associate to form dimers in 0.01 M aluminum lactate buffer (pH 3.1).},
 pages = {17--20},
 title = {ゲルろ過クロマトグラフィーによって認められる低分子量グリアジンの解離・会合},
 volume = {5},
 year = {2013},
 yomi = {ダンノ, ゲンイチ}
}