Effect of Acetylation of Ovalbumin on Its Adsorption Behavior at Solid/Liquid Interface

スポンサーリンク

概要

• 論文の詳細を見る

• This paper reports the effect of modification of lysine residues on the adsorption of ovalbumin at alumina/water interface. It has been shown that the pH dependence of the adsorption changes on acetylation of lysine. Thus at pH 7.6 acetylated ovalbumin does not show any affinity for alumina surface although unmodified protein does. It seems that although electrostatic interactions are operative, surface unfolding of proteins and surface hydrophobicity of protein also control the adsorption of ovalbumin onto alumina.

• 社団法人日本農芸化学会の論文
• 1996-10-23

著者

• Matsudomi Naotoshi

  Faculty Of Agriculture Yamaguchi University

• Bhaduri Anuradha

  Department Of Chemistry Bose Institute

• DAS Kali

  Mason Institute of Ophthalmology, University of Missouri-Columbia

• Das Kali

  Mason Institute Of Ophthalmology University Of Missouri-columbia

関連論文

• Catalytic Role of Mn(IV) Oxide in the Formation of Humic-Enzyme Complexes in the Soil Ecosystem
• Effect of Acetylation of Ovalbumin on Its Adsorption Behavior at Solid/Liquid Interface

スポンサーリンク