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Isolation and Purification of ABA Binding Protein from Abaxial Epiderm of Vicia faba Leaf

Abscisic acid (ABA) was efficiently cross_linked to Sepharose 4B (6～8 mmol ABA/L gel) by an arm of 10_atom carbon chain. Solubilized ABA_BP (ABA binding protein) was allowed to bind to the gel, while unrelated proteins were removed by washing with a gradient of NaCl buffer. The ABA_BP was eluted with 1 mmol/L ABA. Since ABA at high concentration can interfere with both the binding activity assay and protein analysis, the fractions eluted with ABA were passed through a Sephadex G_25 column to remove the ABA. Fractions containing the binding activity were pooled, concentrated with ultra_filtration. The maximum binding capacity ( B MAX ) of the purified ABA_BP was 58.33 nmol/g protein, and the K d was 21 nmol/L, with an approximately 112 folds increase of purity. SDS_PAGE identification of the purified ABA_BP revealed a major protein band with a molecular weight of about 44.2 kD, and a purity of approximately 90%.