The surface of aerosils – substances representing highly disperse nontoxic silica gels – is characterized by a very large area and a specific morphology. These factors account for the high adsorption capacity of aerosils with respect to proteins, enzymes, exoand endotoxins, and microorganisms. The absence of developed pores ensures a high rate of adsorption on the aerosil surface, which makes these media promising sorbents and carriers for immobilization of a wide spectrum of biologically active substances [1]. Sorption methods are used in the course of specific immunotherapy for the immobilization of allergens. Adsorbents used for such purposes include both inorganic (calcium phosphate [2, 3], aluminum hydroxide and phosphate [4]) and organic (L-tyrosine [5]) media; it was also suggested to use activated charcoal as a metric for diagnostic purposes [3]. The aim of this work was to study the process of immobilization of some pollen and food-born allergens on aerosil. We have studied the properties of A-380 aerosil, which had never been used before as a medium for allergen immobilization. This sorbent, obtained from the Institute of Surface Chemistry (National Academy of Sciences of Ukraine, Kiev), is a highly disperse nonporous silica gel with a specific surface of 380 m g, an average particle size of 7 nm, and a surface concentration of silicon atoms of 5.09 mmole g. The main adsorption centers on the aerosil surface are silanol groups (SiOH2 ). The experiments were performed with commercial preparations of rye pollen allergen (RPA) and egg-white allergen (EWA) in the form of aqueous-salt solutions obtained from the “Immunolog” Company (Vinnitsy), which were standardized with respect to protein nitrogen (PNU cm) and stabilized with 0.4% of phenol. RPA and EWA are representatives of the wide classes of pollen and food-born allergens, which are used both for diagnostic purposes and for specific immunotherapy [6, 7] in the complex treatment of allergic disorders. These agents are widespread and characterized by high allergen activity. As is known, the main allergen components in both rye pollen (molecular weight, 38 – 40,000) and in egg-white albumin are glycoproteins (lysozyme, ovalbumin, avomucoid). We have studied the dependence of the allergen adsorption on the protein carrier ratio and the time. The content of
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