Purification of Mutant Forms of beta-glucosidase (His)6Zm-p60.1) Z. mays

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62156489%3A43210%2F08%3A00141770" target="_blank" >RIV/62156489:43210/08:00141770 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Purification of Mutant Forms of beta-glucosidase (His)6Zm-p60.1) Z. mays
Original language description
beta-Glucosidases serve different roles in planta and indeed we find that plants have several different groups of this enzyme. Some of them can release active zeatin from zeatin-O-glucoside, a cytokinin conjugate thought to be the transport or storage form. One such enzyme is Zm-p60.1 from Zea mays. We have over-expressed the cDNA encoding Zm-p60.1 in E. coli and subsequently purified the recombinant protein using a purification (Zouhar et al., 1999, Filipi, 2007, Dopitova et al., 2008). It was necessary to confirm purity of wild-type, as well as mutant forms (F461L, F193A, F200K, W373K and E401D), because of its biochemical data interpretation. Unfortunately, low molecular ballast proteins were still presented in the active (dimeric) fractions of enzyme, thus the purification routine (Filipi, 2007) have been supplemented with other second gel filtration run. By addition with second gel chromatography step, enzymes yield in high homogeneity without any ballast proteins. Moreover, we ha
Czech name
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Czech description
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Project
<a href="/en/project/LC06034" target="_blank" >LC06034: Regulation of morphogenesis of plant cells and organs</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2008
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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