Production and Characterization of Monoclonal Antibodies to Rye (Secale cereale) Phytochrome

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Abstract
Six clones that produce monoclonal antibody (mAb) to large rye (Secale cereale cv. 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 × 10−4 mg/ml to 5 × 10−6 mg/ml, liter being defined as the concentration giving 50% binding 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 PR and PFR were indistinguishable in radioimmunoassay. Two of the mAbs reacted with large oat (Avena saliva cv. Almighty) phytochrome, but none reacted with large pea (Pisum sativum cv. 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 phytochrome.

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