Acid denaturation of mustard 12S protein.
The effect of low pH on the molecular properties of mustard 12S protein has been studied by the techniques of ultracentrifugation, viscometry, electrophoresis, turbidimetry, u.v. difference spectroscopy, fluorescence spectroscopy and circular dichroism. Ultracentrifugation and electrophoresis experiments indicated dissociation of the protein in the pH range 5.0 to 3.0 and below this pH reaggregation was indicated. Viscosity, turbidimetry, u.v. difference spectroscopy, fluorescence spectroscopy and circular dichroism studies showed that denaturation of the protein occurred between pH 5.0 and 3.0 and refolding at pH values below 3.0.
D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D009149:Mustard Plant; D010940:Plant Proteins; D010946:Plants, Medicinal; D011487:Protein Conformation; D011489:Protein Denaturation; D012639:Seeds / Q000032:analysis*; D013050:Spectrometry, Fluorescence; D014783:Viscosity
D010940:Plant Proteins