Structure and properties of water-soluble protein derivatives and hydrophilic polymers

Abstract

The interaction of proteins (as illustrated by ovomucoid of duck's egg protein) and their unsaturated derivatives with the redox system ammonium persulphate-tetramethylethylene diamine has been studied. Such interaction results in the formation of water-soluble protein products with raised MM. The main contribution to this reaction is made by recombination of the macroradicals formed on interaction of the protein molecules with the primary radicals. The introduction into the studied system of low molecular mass comonomers changes the character of the process underway: in this case a decisive contribution to the formation of HMCs is made by the chain propagation reaction. The influence of the conditions of polymerization and the nature of the hydrophilic comonomer on the biological activity of the products formed is shown and ideas advanced on the causes of change in the activity of the water-soluble protein derivative and hydrophilic polymers as a function of the rigidity of the polymer chain.