Abstract
Antisera for the radioimmunoassay of steroid glucuronides have in the past been raised against immunogens in which the glucuronide has been attached to a protein via its carboxylic group. Such antisera do not discriminate well between the glucuronide and the unconjugated free steroid. In order to maximise this discrimination we have synthesized immunogens in which the triacetoxy methyl ester of the steroid glucuronide has been attached to protein unequivocally by a carboxymethyloxime bridge. This immunogen was then deprotected to expose the glucuronide. Deprotection was achieved by two methods; firstly by an in vivo deprotection of the immunogen in rabbits and secondly by selective hydrolysis of the immunogen prior to immunization. All antibodies raised against these immunogens possessed high affinity and discriminated well between the free steroid and the steroid glucuronide.
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