Abstract
The adsorption of several proteins onto latex particles was investigated using a series of polymer latices having the same particle size but with particle surfaces of different chemical structure. The latices were prepared by modification of a styrene—acrylamide copolymer latex. In addition, a polystyrene latex was used to measure the contribution of a hydrophobic surface to the adsorption. With respect to the type of latex, in general, the adsorption of proteins decreased in the order: styrene—acrylamide copolymer latex < amphoteric latex < slightly carboxylated latex < highly carboxylated latex < polystyrene latex, but some changes in the order were observed, dependent on the flexibility of the chain conformation, the polarity, and the molecular weight of the proteins and, in the case of amphoteric latex, on the ratio of amino to carboxyl groups on the particle surface. The enzyme activity of peroxidase when adsorbed on the particles was also investigated.
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