Salt-induced Reconstitution of β-Conglycinin from Its Thermal Dissociates

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The salt-free heat denaturated β-conglycinin, heated to 99°C for 5 min, exhibited dissociation of the protein into subunits (α, α and β). Heat-induced dissociates could be converted to β-conglycinin with an increase in ionic strength of the protein solution. The reassociation of these dissociates depended on the salt concentration and on the species of the constituent subunits. Adding salt above 0.1 M NaCl favored reassociation of the thermal dissociates. The β subunit has a tendency to form an aggregate of higher molecular size, while the α and α subunits have an ability to form the 7S aggregate. Reconstituted β-conglycinin possessed the characteristic of 7S ⇔ 9S interconversion with a change of ionic strength, which has been considered as a feature of native conglycinin. The restoration of electrophoretical mobility, ultracentrifugal characteristics and the secondary structure of CD properties was distinct evidence supporting the reconstitution of β-conglycinin from its thermally denatured state. However, the reconstituted conformation differed from the native β-conglycinin in its quantitative precipitin curve and ultraviolet difference spectrum.