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http://purl.uniprot.org/citations/12777048http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12777048http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12777048http://www.w3.org/2000/01/rdf-schema#comment"An alpha-L-fucosidase purified from pea (Pisum sativum L. cv Alaska) epicotyl was previously described as a cell wall enzyme of 20 kDa that hydrolyses terminal alpha-L-fucosidic linkages from oligosaccharide fragments of xyloglucan. cDNA and genomic copies were further isolated and sequenced. The predicted product of the cDNA and the genomic clone (fuc1), was a 20 kDa protein containing a signal peptide and five cysteines. This was the first alpha-L-fucosidase gene to be cloned in plants but its fucosidase activity has not been demonstrated. Here, our biochemical and immuno analyses suggest that fuc1 does not encode an alpha-L-fucosidase. Pea fuc1 expressed in Escherichia coli, insect cells and Arabidopsis thaliana produced recombinant proteins without alpha-L-fucosidase activity. Pea plants had endogenous alpha-L-fucosidase activity, but the enzyme was not recognised by an antibody produced against recombinant FUC1 protein expressed in E. coli. In contrast, the antibody immunoprecipitated a 20 kDa protein which was inactive. By chromatographic analysis of pea protein extracts, we separated alpha-L-fucosidase-active fractions from the 20 kDa protein fractions. We conclude that the alpha-L-fucosidase activity is not attributable to the 20 kDa FUC1 protein. A new function for fuc1 gene product, now named PIP20 (for protease inhibitor from pea) is proposed."xsd:string
http://purl.uniprot.org/citations/12777048http://purl.org/dc/terms/identifier"doi:10.1023/a:1023053101938"xsd:string
http://purl.uniprot.org/citations/12777048http://purl.org/dc/terms/identifier"doi:10.1023/a:1023053101938"xsd:string
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/author"Puigdomenech P."xsd:string
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/author"Puigdomenech P."xsd:string
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/author"Martinez I."xsd:string
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/author"Martinez I."xsd:string
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/author"Giralt E."xsd:string
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/author"Giralt E."xsd:string
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/author"Tarrago T."xsd:string
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/author"Tarrago T."xsd:string
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/author"Torrent M."xsd:string
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/author"Torrent M."xsd:string
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/author"Ludevid D."xsd:string
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/author"Ludevid D."xsd:string
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/author"Codina A."xsd:string
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/author"Codina A."xsd:string
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/name"Plant Mol. Biol."xsd:string
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/name"Plant Mol. Biol."xsd:string
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/pages"877-884"xsd:string
http://purl.uniprot.org/citations/12777048http://purl.uniprot.org/core/pages"877-884"xsd:string