Extracellular beta-glucosidase activity in barley involved in the hydrolysis of ABA glucose conjugate in leaves

Abscisic acid conjugate concentrations increased in barley xylem sap under salinity, whereas it remained at a low level in the intercellular washing fluid (IWF) of barley primary leaves (Hordeum vulgare cv. Gerbel). Here it is shown that IWF contains beta-glucosidase activity which releases abscisic...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 51(2000), 346 vom: 08. Mai, Seite 937-44
1. Verfasser: Dietz, K J (VerfasserIn)
Weitere Verfasser: Sauter, A, Wichert, K, Messdaghi, D, Hartung, W
Format: Aufsatz
Sprache:English
Veröffentlicht: 2000
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Sodium Chloride 451W47IQ8X Abscisic Acid 72S9A8J5GW beta-Glucosidase EC 3.2.1.21 Glucose IY9XDZ35W2
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245 1 0 |a Extracellular beta-glucosidase activity in barley involved in the hydrolysis of ABA glucose conjugate in leaves 
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520 |a Abscisic acid conjugate concentrations increased in barley xylem sap under salinity, whereas it remained at a low level in the intercellular washing fluid (IWF) of barley primary leaves (Hordeum vulgare cv. Gerbel). Here it is shown that IWF contains beta-glucosidase activity which releases abscisic acid (ABA) from the physiologically inactive ABA-glucose conjugate pool in the leaf apoplast. The following data support this conclusion and give the first biochemical and physiological characterization of the extracellular glucosidase activity in barley. Free ABA was released by the incubation of ABA glucose ester with IWF. The product exhibited the retention time of authentic ABA upon separation by thin layer chromatography and was identified by ABA-ELISA. p-Nitrophenol-beta-D-glucopyranoside (pNPG) was used as the substrate for beta-glucosidases. The K(M)(pNPG) was 1.8 mmol l(-1). The activity was affected by ABA glucopyranoside in a competitive type of inhibition with a K(I) of 400 micromol l(-1). Various hormone conjugates were compared with respect to their inhibitory effect on beta-glucosidase activity. Inhibition was highest for the ABA glucopyranoside and the zeatin riboside, but insignificant for ABA methyl ester and zeatin-9-beta-D-glucoside. The specific activity of the beta-glucosidase was 16-fold greater in IWF as compared to crude leaf extracts confirming its extracellular compartmentation. The activity of beta-glucosidase was strongly increased after growth in hydroponic medium supplemented with NaCl. The data support the hypothesis that the glucose conjugate is a long-distance transport form of ABA 
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700 1 |a Sauter, A  |e verfasserin  |4 aut 
700 1 |a Wichert, K  |e verfasserin  |4 aut 
700 1 |a Messdaghi, D  |e verfasserin  |4 aut 
700 1 |a Hartung, W  |e verfasserin  |4 aut 
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