The ABA Binding Proteins and Their Properties in Grapevine Fruit

in HortScience
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  • 1 1College of Plant Science and Technology, China Agricultural Univ., Beijing 100094, P.R. China
  • | 2 2Florida A&M Univ., Center for Viticulture Sciences Tallahassee, FL 32307

The abscisic acid (ABA) has a key role in the regulation of grapevine fruit ripening, but the cellular and molecular biological mechanism of the hormone action in the fruit ripening remains unknown. By means of differential centrifugation, microsomes were prepared from Kyoho grapevine (Vitis vinifera L. × V. Labrusca L.) berries, and using the microsomes, we have obtained evidence for the occurrence of specific ABA-binding sites on the membranes with the microvolume radio-ligand binding assay. The binding sites had saturability, high affinity, and low capacity. The results of trypsin and dithiothreitol treatments to the microsomes suggested that ABA binding sites had the properties of proteins that might have disulfide group located at or near the binding site. The binding maximum amount of ABA in the microsomes was at pH 6.0 and the activity of ABA binding proteins was higher at 25 than at 0°C (temperature). The amount of ABA bound reached 54% of the ABA binding maximum (Bmax) for 10 minutes of incubation and Bmax reached for 30 minutes. The dissociation constant (Ka) and Bmax of ABA binding proteins in the microsomes were 17.5 nmol/L and 98.4 fmol/mg protein, respectively.

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