2228-72-0Relevant articles and documents
UV-INDUCED CROSS-LINKING OF ABSCISIC ACID TO BINDING PROTEINS
Cornelussen, Mathus H. M.,Karssen, Cees M.,Loon, Leendert C. van
, p. 959 - 968 (1995)
Conditions for UV-induced cross-linking of abscisic acid (ABA) through its enone chromophore to binding proteins are evaluated.The effects of a UV-light band between 260 and 530 nm of both unconjugated and protein-conjugated ABA, as well as on anti-ABA antibodies as models of ABA-binding proteins were determined.UV irradiation caused both isomerization and photolysis of ABA, but increasing the lower irradiation boundary to 345 nm strongly reduced photolysis and largely prevented isomerization.When conjugated to alkaline phosphatase (AP), ABA remained stable when using either a 320 or a 345 mn filter.At these wavelenghts both bonding of ABA to antibodies as well as AP enzymatic activity were maintained.UV-induced cross-linking of monoclonal anti-ABA antibodies to immobilized ABA was analysed by immunoassays.Optimal cross-linking was achieved after a 5 min irradiation period at 0 deg C, using a long pass, cut-on filter to quench wavelengths below 290 nm.This cross-linking faithfully reflected cognate binding activity.
Synthesis and biological activity of abscisic acid esters
Wan, Chuan,Zhang, Yuanzhi,Yang, Dongyan,Han, Xiaoqiang,Li, Xiuyun,Li, Hong,Xiao, Yumei,Qin, Zhaohai
, p. 267 - 272 (2015/06/22)
Abstract 16 ABA esters including 11 new compounds were prepared by two different esterification routes. All the structures of ABA esters were confirmed by 1H NMR, 13C NMR and HRMS. Their biological activity and hydrolysis stability were investigated. Fortunately, there were 15 and 9 compounds which displayed much better or nearly the same inhibition activity for rice seedling growth and Arabidopsis thaliana seed germination compared to ABA, respectively. Especially, compounds 2d and 2g showed better biological activities than ABA in the three tests. Moreover, we found that chemical hydrolysis ability of the esters in vitro had little relationship to their biological activity.
Resolution of (+)-abscisic acid using an Arabidopsis glycosyltransferase
Lim, Eng-Kiat,Doucet, Charlotte J.,Hou, Bingkai,Jackson, Rosamond G.,Abrams, Suzanne R.,Bowles, Dianna J.
, p. 143 - 147 (2007/10/03)
Abscisic acid (ABA) can exist as two enantiomers, with (+)-ABA as the naturally occurring form. Typically, both enantiomers occur in chemical preparations and both can be modified in the plant to their respective glucose esters. To identify glycosyltransferases capable of discriminating between the different forms of ABA, the Family 1 enzymes of Arabidopsis thaliana were screened for activity towards (±)-ABA. Eight enzymes were found to recognise the plant hormone, with one UGT71B6 showing enantioselective glucosylation towards (+)-ABA. UGT71B6 was used in a whole-cell biocatalysis system as a means of separating (+)- and (-)-ABA, thereby offering an alternative to chemical synthesis for the production of pure (+)-ABA.