نتایج جستجو برای: glucuronidase (gus) activity
تعداد نتایج: 1137339 فیلتر نتایج به سال:
The GUS gene of E. coli, encoding b-glucuronidase, has been widely used as a reporter gene in plant transformation. However, b-glucuronidase activity in transgenic wheat leaf or root tissue is rarely observed or reported. To address this question, we investigated three wheat lines transformed with the GUS reporter gene. We found all three lines expressed GUS mRNA as well as b-glucuronidase prot...
A β-glucuronidase variant, GUS-TR3337, that was obtained by directed evolution exhibited higher thermostability than the wild-type enzyme, GUS-WT. In this study, the utility of GUS-TR337 as an improved reporter was evaluated. The corresponding gus-tr3337 and gus-wt genes were independently cloned in a plant expression vector and introduced into Arabidopsis thaliana. With 4-MUG as a substrate, p...
camv 35s promoter activity has not been analysed in different stages of growth in oil-seed (b. napus). higher plants lack intrinsic β-glucuronidase activity, thus enhancing the sensitivity with which measurements can be made. the binary transformation vector pvw432 (buchanan-wollaston, unpublished), carrying the gus gene fused to the camv 35s promoter, was used to test transformation efficienci...
Chimeric mice were produced by aggregating 2 embryos, each of which was homozygous for a different structural allele of the enzyme /?-glucuronidase. The two alleles used were Gus, the 'wild-type' allele, and Gus, an allele whose gene product shows decreased activity in all tissues as well as decreased heat stability. Staining of untreated adult chimeric livers for glucuronidase activity reveale...
Glycosyl hydrolases hydrolyze the glycosidic bond in carbohydrates or between a carbohydrate and a non-carbohydrate moiety. beta-glucuronidase (GUS) is classified under two glycosyl hydrolase families (2 and 79) and the family-2 beta-glucuronidase is reported in a wide range of organisms, but not in plants. The family-79 endo-beta-glucuronidase (heparanase) is reported in microorganisms, verteb...
We constructed a protein expression vector with an improved enoA promoter that harbored 12 tandem repeats of the cis-acting element (region III) of Aspergillus oryzae. The improved promoter yielded reporter beta-glucuronidase (GUS) activity approximately 30-fold of the original promoter. Northern blot analysis confirmed that GUS expression was increased at the transcriptional level. The transfo...
We cloned the isovaleryl-CoA dehydrogenase (IVD)-encoding gene from Aspergillus oryzae. The promoter of ivdA was subjected to beta-glucuronidase (GUS) reporter assays in which certain amino acids were used as a major carbon source. L-leucine most strongly induced GUS-activity, while in the case of L-glutamate, significantly low activity was found, indicating that ivdA transcription was strongly...
To investigate the regulation of gene expression during male gametophyte development, we analyzed the promoter activity of two different genes (LAT52 and LAT59) from tomato, isolated on the basis of their anther-specific expression. In transgenic tomato, tobacco and Arabidopsis plants containing the LAT52 promoter region fused to the beta-glucuronidase (GUS) gene, GUS activity was restricted to...
We have characterized the 5' region of the rice actin 1 gene (Act1) and show that it is an efficient promoter for regulating the constitutive expression of a foreign gene in transgenic rice. By constructing plasmids with 5' regions from the rice Act1 gene fused to the coding sequence of a gene encoding bacterial beta-glucuronidase, we demonstrate that a region 1.3 kilobases upstream of the Act1...
In poplars (Populus), bspA encodes a 32-kD bark storage protein that accumulates in the inner bark of plants exposed to either short-day (SD) photoperiods or elevated levels of nitrogen. In this study, poplars transformed with a chimeric gene consisting of the bspA promoter fused to beta-glucuronidase (uidA) were used to investigate the transcriptional regulation of the bspA promoter. Photoperi...
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