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The Journal of Immunology, 1973, 110: 667-673.
Copyright © 1973 by The American Association of Immunologists, Inc.
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A Measurement of the Specificities of Antibodies to Morphine-6-Succinyl-BSA by Competitive Inhibition of 14C-Morphine Binding1

Bruce H. Wainer2, Frank W. Fitch, Josef Fried and Richard M. Rothberg3

Departments of Pediatrics, Pathology and Chemistry, University of Chicago, Chicago, Illinois 60637

Abstract

Antisera reacting with morphine were produced in rabbits by immunization with morphine-6-succinyl-bovine serum albumin. The antibody assay employed ammonium sulfate precipitation of antibody-14C-morphine complexes. The specificities of the sera were measured by prior incubation of appropriate serum dilutions with increasing concentrations of various unlabeled opioids before the addition of 14C-morphine. Opioids differed in their ability to inhibit interaction of 14C-morphine and antibody; concentrations inhibiting binding of 88 pmol/ml of 14C-morphine by 50% were: morphine-6-hemisuccinate, 0.052 nmol/ml; heroin, 0.10 nmol/ml; morphine, 0.11 nmol/ml; codeine, 0.16 nmol/ml; hydromorphone, 0.50 nmol/ml; nalorphine, 2.1 nmol/ml; meperidine, 80.0 nmol/ml; naloxone, 30% inhibition at 1.0 x 103 nmol/ml. Variations in the ability to inhibit 14C-morphine binding were related to the nature of the structural dissimilarities between the competing compound and the homologous hapten. Differences in I50 values for the opioids studied were reflections of inhibition curves with differing slopes. Such observations allow the possibility of both qualitative and quantitative analyses in assay systems.

Footnotes

1 This work was supported by United States Public Health Service Research Grant 1 RO3 MH-21 544-01 and the Louis Block Fund, The University of Chicago.

2 Recipient of United States Public Health Service Training Grant 5 TO 5 GMO 1939-04 (MSTP) from the University of Chicago.

3 Recipient of a United States Public Health Service Research Career Development Award 5-K4-AI-13,936 38,899.






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