Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Plant Physiology 95:46-51 (1991)
© 1991 American Society of Plant Biologists

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Molecular Biology and Gene Regulation

Monoclonal Antibody Recognition of Abscisic Acid Analogs

Mary K. Walker-Simmons, Martin J. T. Reaney, Stephen A. Quarrie, Pierdomenico Perata, Paolo Vernieri and Suzanne R. Abrams

U.S. Department of Agriculture, Agriculture Research Service, Wheat Genetics, Quality, Physiology and Disease Research, Pullman, Washington 99164-6420, Crop Science Department, University of Saskatchewan, Saskatoon, SK Canada S7N 0W0, Cambridge Laboratory, John Innes Centre for Plant Science Research, Colney Lane, Norwich N4R 7UJ, United Kingdom, Dipartimento di Biologia delle Piante Agrarie, Universita di Pisa, Viale delle Piagge 23, 56100 Pisa, Italy, Plant Biotechnology Institute, National Research Council of Canada, 110 Gymnasium Place, Saskatoon, SK Canada S7N 0W9

Specificities of three monoclonal antibodies (15-I-C5, DBPA 1, and MAC 62) raised against the plant hormone (S)-(+)-abscisic acid (ABA) have been compared. Immunological cross-reactivities against fifteen biologically active analogs of ABA were measured. The ABA analogs were altered at one or more of four positions: the double bonds in the ring, at C-2 C-3 and at C-4 C-5, and in the oxidation level at C-1. Several analogs were optically active with chiral centers at C-1' and C-2'. For cross-reactivity, all three monoclonal antibodies required the carboxylic acid group, and the cis configuration of the double bond at C-2 C-3 of the ABA molecule. Monoclonals 15-I-C5 and DBPA 1 required the entire ABA sidechain from the C-1 to C-1', but these monoclonals did cross-react with analogs with the ring double bond reduced and the C-2' methyl cis to the sidechain. Only MAC 62 recognized analogs containing an acetylene at C-4 C-5. MAC 62 had more strict requirements for the ring double bond, but gave some cross-reactivity with acetylenic analogs having a saturated ring. All three monoclonals had higher specificity for analogs having the same absolute configuration at C-1' as (S)-(+)-ABA. This work provides new information about the spatial regions of the ABA molecule that elicit immunological recognition, and serves as a basis for future investigations of the ABA receptor using ABA analogs and anti-idiotypic antibodies.





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