Pregled bibliografske jedinice broj: 241868
Auxin-amidohydrolase in wheat: cloning, expression and substrate specificity
Auxin-amidohydrolase in wheat: cloning, expression and substrate specificity // Knjiga sažetaka, VI susret mladih kemijskih inženjera / Božić, Slaven ; Hraste, Marin ; Kurtanjek, Želimir ; Pejčić, Marijan ; Vasić-Rački, Đurđa (ur.).
Zagreb: Hrvatsko društvo kemijskih inženjera i tehnologa (HDKI) ; Fakultet kemijskog inženjerstva i tehnologije Sveučilišta u Zagrebu, 2006. str. 51-51 (poster, nije recenziran, sažetak, znanstveni)
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Naslov
Auxin-amidohydrolase in wheat: cloning, expression and substrate specificity
Autori
Tomašić, Ana ; Magnus, Volker ; Salopek-Sondi, Branka
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
Knjiga sažetaka, VI susret mladih kemijskih inženjera
/ Božić, Slaven ; Hraste, Marin ; Kurtanjek, Želimir ; Pejčić, Marijan ; Vasić-Rački, Đurđa - Zagreb : Hrvatsko društvo kemijskih inženjera i tehnologa (HDKI) ; Fakultet kemijskog inženjerstva i tehnologije Sveučilišta u Zagrebu, 2006, 51-51
Skup
VI susret mladih kemijskih inženjera
Mjesto i datum
Zagreb, Hrvatska, 23.02.2006. - 24.02.2006
Vrsta sudjelovanja
Poster
Vrsta recenzije
Nije recenziran
Ključne riječi
auxin; amidohydrolase; indole-3-acetic acid; IAA; indole-3-acetic acid; IBA; indole-3-butyric acid; gene cloning
Sažetak
The wheat IBA-amidohydrolase, TaIAR3, was investigated. The TaIAR3 gene is an ortholog of the Arabidopsis IAA-amidohydrolase and has been isolated from winter wheat (Triticum aestivum L. cv. Caledonia). The complete cDNA of TaIAR3 was cloned into the pETBlue-2 vector and protein expression was obtained in E. coli. In order to determine enzyme activity and substrate specificity, the bacterial cell lysate was processed for biochemical reaction with the substrate, IBA-Ala, for 1, 2, 4, and 6 hours, extracted with ethyl acetate, evaporated to dryness in a stream of nitrogen and resuspended in methanol for HPLC analysis. The HPLC separation confirmed hydrolase activity in the bacterial homogenate, Furthermore, it was shown that specific cleavage of IBA-Ala, which is an inactive form of auxin, affords free, physiologically active, IBA. This leads to the conclusion that auxin-amidohydrolase may be involved in auxin metabolism, specifically controlling the release of active auxin.
Izvorni jezik
Engleski
Znanstvena područja
Biologija
