過酸化水素の低温プラズマ放電処理した際に生成する活性種による蛋白質の構造変化に関する研究 : モデルとして用いたアルブミンの構造変化

Abstract

"It is important to study how the molecular structures of protein is affected by the active species generated from hydrogen peroxide in the plasma discharging field at low temperature." Then, the simple simulations have been done using albumin (MW: ca. 67,000) as the model for protein. Two surprising phenomena were observed. First, only one peak was observed in the molecular weight range of ca. 330,000 on the Gel Permeation Chromatogram of albumin after the sterilizing treatment. Second, the specific decreasing the lysine component in albumin molecule was observed by the liquid chromatographic amino acid analysis technique. It has been thought the following reaction mainly might be proceeded. -NH_2+\OH→-NH\+H_2O Dehydration Reaction (in lysine site) -HN\+\NH-→-HN-NH-, Intermolecular Crosslinking Reaction. Then, the single peak on the Gel Permeation Chromatogram of albumin after the sterilizing treatment might be reflected to the formation of pentmer of albumin by the above the intermolecular crosslinking reaction mechanism. The characteristic changes of 20 species of the essential amino acids treated by the above mentioned experimental condition have also discussed by the high performance liquid chromatographic technique.