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Plant and Cell Physiology, 1984, Vol. 25, No. 6 1059-1068
© 1984

Article

Production and Characterization of Monoclonal Antibodies Which Distinguish Different Surface Structures of Pea (Pisum sativum cv. Alaska) Phytochrome

Akira Nagatani1,3, Kotaro T. Yamamoto3, Masaki Furuya1,3, Tetsuo Fukumoto2 and Akira Yamashita2

1Department of Biology, Faculty of Science, University of Tokyo Hongo, Tokyo 113, Japan
2Department of Anatomy, Hamamatsu University School of Medicine Hamamatsu, Shizuoka 431-31, Japan
3Division of Biological Regulation, National Institute for Basic Biology Okazaki, Aichi 444, Japan

Eight monoclonal antibodies to pea 114,000 dalton phytochrome (mAP-1 to mAP-8) were produced by fusing spleen cells from immunized BALB/c mice with NS-1 myeloma cells. Antibody production by mAP-1 to mAP-7 was detected by cellular radioimmunoassay using sheep red blood cells coated with pea phytochrome. Relative binding positions of these mAPs were determined using a competitive binding assay, and at least 6 different antigenic regions were defined on the 114,000 dalton chromopeptide. Location of the regions in relation to the chromophore was studied by examining the cross-reactions of the relevant mAPs with chromophore-containing proteolytic fragments (62,000, 37,000 and 24,000 daltons) of phytochrome. The following cross-reactions were observed; mAP-1 with 62,000, mAP-6 and mAP-7 with 62,000, 37,000 and 24,000. Only mAP-7 caused "spectral denaturation" of phytochrome. All mAPs reacted with PR and PFR with similar affinity. These mAPs will be useful probes in future studies for detecting each site of the apoprotein of phytochrome. By using another screening method, namely radioimmunoassay with antigen-coupled Sepharose 4B, mAP-8 was also obtained.

(Received May 4, 1984; Accepted June 25, 1984)
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