Six clones that produce monoclonal antibody (mAb) to large rye (Secale cerealecv. Haru-Ichiban) phytochrome were established by fusing spleen cells from immunized BALB/c mice with NS-1 myeloma cells. The binding characteristics of the mAbs to rye phytochrome were analyzed by radioimmunoassay with sheep red blood cells coupled with rye phytochrome as the target cells. The mAbs had titers that ranged from 2×10−4mg/ml to 5×10−6mg/ml, liter being defined as the concentration giving 50binding in the radioimmunoassay.All 6 mAbs reacted with small rye phytochrome, proteolytic fragment of phytochrome (mol wt 62,000), but their modes of reaction varied somewhat. None affected the absorption spectra of rye phytochrome by binding, and their affinities to PRand PFRwere indistinguishable in radioimmunoassay. Two of the mAbs reacted with large oat (Avena salivacv. Almighty) phytochrome, but none reacted with large pea (Pisum sativumcv. Alaska) phytochrome. Thus, the mAbs obtained were classifiable into two categories based on differences in their cross-reactivity to oat phytochrome and their binding affinities to large and small rye phytoc
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