| Abstract: | The 11S-globulin has a complex stable quaternary structure in the formation of which three types of subunits participate. The aim of the work was to determine what forces form and stabilize the quaternary structure of this protein. The products of the maleylation and acetylation of the 11S-globulin and also the stability of the native 11S-globulin in the presence of ionic and nonionic detergents were investigated by disk electrophoresis. It was shown that hydrophobic interactions play a deciding role in the formation and stabilization of the quaternary structure of the 11S-globulin.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 4, pp. 554–557, July–August, 1979. |
