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United States Department of Agriculture

Agricultural Research Service

Title: Affinity Probes for Isolation of Abscisic Acid-Binding Proteins

item Nyangulu, James - ST FRANCIS XAVIER UNIV
item Galka, Marek - UNIV OF CALGARY
item Jadhav, Ashok - UNIV OF CALGARY
item Gai, Yuanzhu - UNIV OF SASKATCHEWAN
item Graham, Cindy - UNIV OF CALGARY
item Cutler, Adrian - UNIV OF SASKATCHEWAN
item Taylor, David - UNIV OF SASKATCHEWAN
item Banowetz, Gary
item Abrams, Suzanne - UNIV OF SASKATCHEWAN

Submitted to: Journal of the American Chemical Society
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: December 31, 2004
Publication Date: June 30, 2005
Citation: Nyangulu, J.M., Galka, M.M., Jadhav, A., Gai, Y., Graham, C.M., Nelson, K.M., Cutler, A.J., Taylor, D.C., Banowetz, G.M., Abrams, S.R. 2005. Affinity probes for isolation of abscisic acid-binding proteins. Journal of the American Chemical Society. v.127. p.1662-1664.

Interpretive Summary: The plant hormone, abscisic acid (ABA) regulated many agronomically important process during the development of many crop plants including seed formation and responses to environmental stresses. The mechanism by which ABA binds to plant components to participate in these physiological processes remains unknown. This study developed a probe to isolate plant proteins capable of binding ABA so that further progress can be made in understanding the pathways by which ABA interacts with plant components to impact stress tolerance and plant development.

Technical Abstract: An affinity-based method that employed a biologically active derivative of abscisic acid (ABA) linked to Sepharose was developed for isolation of ABA-binding proteins from plant extracts. The receptor probe incorporated all the functional groups of ABA required for binding to an anti-(+)-ABA monoclonal antibody including stereochemistry at C-1, the acid functional group on the side chain, and the ketone on the ring. The synthesis of the bioactive, biotinylated probe is described and validation of the probe was provided by isolation of ABA-8'hydroxylase.

Last Modified: 4/22/2015
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