Catalytic activity of conjugates of peroxidase with progesterone in aqueous and micellar media in the presence of antibodies against progesterone
Eremin, A.N.; Metelitsa, D.I.
Bioorganicheskaia Khimiia 15(10): 1326-1333
1989
ISSN/ISBN: 0132-3423 PMID: 2698619 Document Number: 331441
At 22 and 41 degrees C the horseradish peroxidase (HRP) conjugates with progesterone, HRP-PROG-1 and HRP-PROG-2, were obtained by HRP reaction with N-hydroxysuccinimide ester of 3-O-carboxymethyloxime of progesterone. The interaction of these conjugates and unmodified enzyme with antibodies against progesterone was studied in phosphate-citrate buffer pH 3.6 and in the reversed micelles of Aerosol OT and Triton X-45 in heptane. Catalytic function of conjugates in buffered solutions and in reversed micelles increases as result of the conjugates' interaction with antibodies. The free progesterone in reversed micelles competes with HRP-PROG-1 for antibody binding, which may be the basis for homogeneous enzyme-immunoassay of progesterone, depending on the micelle composition, the antibody concentration and temperature.