D. farinae allergen has been modified with formaldehyde and its properties have been studied. This study has demonstrated that the formolation of D. farinae ticks allergen causes changes in isoelectric points of proteins and a shift of protein fraction to acidic pH values: 3.0-4.85; an insignificant decrease in the volume of gel filtration output on a column packed with Sephacryl S-300; a decrease in the esterase activity from 10.5 to 1.8 microM tosylarginine methyl ester/min. per mg of protein. As revealed with the use of microdot enzyme immunoassay, the modified allergen loses its capacity to bind with human specific IgE antibodies in vitro.
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