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옥수수 태생돌연변이체-1 및 정상체의 호분층 (糊紛層) 유출물과 ABA 의 결합
배동규 ( Dong Gyu Bai ),문정선 ( Jung Sun Moon ),( J. D. Smith ) 한국식물학회 1994 Journal of Plant Biology Vol.37 No.2
Aleuroue layers of normal and vp1 mutant maize kernels were extracted and centrifuged at 100,000 g to yield a cytosol fraction. Binding of [^3H]ABA cis, trans (+)ABA to a soluble macromolecular components present in the cytosol was demonstrated by Sephadex chromatography and non-denaturing PAGE. The binding component was of high molecular weight and seems to be an aggregate of proteins. A rapid DEAE-cellulose filter method for assaying bound [^3H]ABA to a soluble protein was adapted. Biding assays were performed with cytosol that had been preheated or incubated with several enzymes, indicating that heat and protease treatments disrupted the binding. This suggested that binding occurred to proteins. Some properties of the ABA binding proteins were described. The [^3H]ABA binding were reduced dramatically when unlabeled ABA was added as a competitor, Suggesting a specific binding of [^3H]ABA. Gel filtration profiles and autoradiogram of [^3H]ABA binding showed no difference in the binding components of Vp1 and vp1/vp1 mutant cytosol, indicating that Vp1 protein is not a sole ABA binding protein.