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Evaluation of the activity of peroxidase conjugates with immunoglobulins isolated by different methods from the sera of the subjects with a history of virus hepatitis A, and at various molar ratios of peroxidase and immunoglobulins showed the activity of immunoperoxidase conjugates to depend upon the method of isolation of immunoglobulin used for conjugation. The most active immunoperoxidase conjugates were obtained with immunoglobulins isolated by a column-free method on sephadex DEAE-50A. When peroxidase with a low specific activity is used, the quality of conjugate may be improved by increasing the amount of the enzyme added in conjugation.
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