Changes in the Shape and Surface Hydrophobicity of Ovalbumin during Its Transformation to s-Ovalbumin

スポンサーリンク

概要

• 論文の詳細を見る

• Intrinsic viscosity, Stokes radius and the hydrophobic coefficient of Keshavarz and Nakai [Biochim. Biophys. Acta, 576, 269 (1979)] were measured to compare the shape and surface hydrophobicity of ovalbumin and s-ovalbumin. Both the intrinsic viscosity and Stokes radius of s-ovalbumin were smaller than those of ovalbumin, which suggests that the configuration of s-ovalbumin became more compact during the ovalbumin-s-ovalbumin transformation. The hydrophobic coefficient of s-ovalbumin was larger than that of ovalbumin, which suggests that the surface hydrophobicity of s-ovalbumin was larger than that of ovalbumin. Further, these properties were measured for ovalbumin samples obtained at various stages of ovalbumin-s-ovalbumin transformation. Changes in the shape and surface hydrophobicity of ovalbumin were not found in the first stage of ovalbumin-s-ovalbumin transformation. They changed rapidly in the last stage of the ovalbumin-5-ovalbumin transformation.

• 社団法人 日本農芸化学会の論文

著者

• NAKAMURA Ryo

  Laboratory of Food Science and Nutrition, Faculty of Agriculture, Tottori University

• ISHIMARU Masuko

  Laboratory of Food Science and Nutrition, Faculty of Agriculture, Tottori University

関連論文

• The Effect of Halogenation of Phe-Phenyl Group of Two Consecutive Phe Residues Present in Neuropeptide Substance P on Its Specific Receptor Interaction
• Changes in the Shape and Surface Hydrophobicity of Ovalbumin during Its Transformation to s-Ovalbumin
• High-precision Binding Assay Procedure of Tachykinin Receptor NK-1 for Highly Potent Substance P Analogs

スポンサーリンク