@article{oai:osaka-aoyama.repo.nii.ac.jp:00000022,
 author = {団野, 源一},
 journal = {大阪青山大学紀要, Journal of Osaka Aoyama University},
 month = {Mar},
 note = {40017399086, Glutenin dispersed in 0.2 M sodium phosphate buffer (pH 7.0) was heated at various temperatures for 15 min. 　Effects of the heat-treatment on the subunit pattern was studied by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). 　No　change in the subunit pattern of glutenin was observed by heating at 120℃. 　A high molecular weight protein which did not migrate into gel matrix during electrophoresis was observed in the glutenin heat-treated at a temperature higher than 130℃. 　All the subunits disappeared by heating at 150℃. 　Increasing the temperature elevated the ratio of soluble fractions in 7.5% trichloroacetic acid (TCA-soluble fraction), and about 50% of glutenin changed into TCA-soluble fractions by heating at 170℃. 　These results suggest that polymerization and decomposition of glutenin subunits occurred simultaneously by heating at high temperatures. (accepted. Oct. 30, 2009)},
 pages = {33--37},
 title = {小麦グルテニンに及ぼす高温加熱の影響},
 volume = {2},
 year = {2009},
 yomi = {ダンノ, ゲンイチ}
}