The behavior of human serum albumin (HSA) and gamma globulins (γG) at the interfaces of poly(styrene/acrolein) latex particles and solvent is described. It is shown how the relative amounts of proteins bound to the latex surfaces by hydrophobic adsorption and by covalent immobilization are affected by the chemical composition of the latex particles. The competition in adsorption of "monomelic", "dimeric" and "oligomeric" HSA is also described. Studies of fluorescently marked HSA and γG at interfaces of latex particles and solvent indicate that, after attachment, protein molecules first lose their internal fluidity and only later change their conformation.In medical and veterinary applications of polymeric materials, it is essential to understand what happens to various macromolecules, vital for functions of an organism, when the macromolecules approach the polymeric surface. One of these applications entails using polymeric latexes and microspheres for diagnostic purposes. Latexes with the appropriate antibodies, adsorbed and/or covalently immobilized at their surfaces, are used for detection of the corresponding antigens in standard agglutination tests (1). Recently, the new, so called "dry tests" have been designed (e.g. the tests for detection of antigens against the HIV and hepatitis viruses (2)). In these tests the only liquid being used is the liquid from the analyzed sample.Regardless of the actual design of the test, it is crucial to establish whether the required biologically active compounds could be adsorbed or covalently immobilized at the surface of the prospective latex particles. Special attention has to be paid to the microheterogenity of the surface of polymeric composite materials, because this often leads to the distribution of the protein attachments to the patches with different chemical composition (3). Not less important is to determine the character and degree of changes occurring in the bioactive molecules upon attachment to the surface. In the 0097-6156/94/0548-0449$06.00/0