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http://purl.uniprot.org/citations/8000004http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8000004http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8000004http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/8000004http://www.w3.org/2000/01/rdf-schema#comment"A protein consisting of 60 kDa subunits (As-P60) was isolated from etiolated oat seedlings (Avena sativa L.) and characterized as avenacosidase, a beta-glucosidase that belongs to a preformed defence system of oat against fungal infection. The enzyme is highly aggregated; it consists of 300-350 kDa aggregates and multimers thereof. Dissociation by freezing/thawing leads to complete loss of enzyme activity. The specificity of the enzyme was investigated with para-nitrophenyl derivatives which serve as substrates, in decreasing order beta-fucoside, beta-glucoside, beta-galactoside, beta-xyloside. The corresponding orthonitrophenyl glycosides are less well accepted. No hydrolysis was found with alpha-glycosides and beta-thioglucoside. An anti-As-P60 antiserum was prepared and used for isolation of a cDNA clone coding for As-P60. A presequence of 55 amino acid residues was deduced from comparison of the cDNA sequence with the N-terminal sequence determined by Edman degradation of the mature protein. The presequence has the characteristics of a stroma-directing signal peptide; localization of As-P60 in plastids of oat seedlings was confirmed by western blotting. The amino acid sequence revealed significant homology (> 39% sequence identity) to beta-glucosidases that are constituents of a defence mechanism in dicotyledonous plants. 34% sequence identity was even found with mammalian and bacterial beta-glucosidases of the BGA family. Avenacosidase extends the occurrence of this family of beta-glucosidases to monocotyledonous plants."xsd:string
http://purl.uniprot.org/citations/8000004http://purl.org/dc/terms/identifier"doi:10.1007/bf00028858"xsd:string
http://purl.uniprot.org/citations/8000004http://purl.org/dc/terms/identifier"doi:10.1007/bf00028858"xsd:string
http://purl.uniprot.org/citations/8000004http://purl.uniprot.org/core/author"Brunner H."xsd:string
http://purl.uniprot.org/citations/8000004http://purl.uniprot.org/core/author"Brunner H."xsd:string
http://purl.uniprot.org/citations/8000004http://purl.uniprot.org/core/author"Gus-Mayer S."xsd:string
http://purl.uniprot.org/citations/8000004http://purl.uniprot.org/core/author"Gus-Mayer S."xsd:string
http://purl.uniprot.org/citations/8000004http://purl.uniprot.org/core/author"Rudiger W."xsd:string
http://purl.uniprot.org/citations/8000004http://purl.uniprot.org/core/author"Rudiger W."xsd:string
http://purl.uniprot.org/citations/8000004http://purl.uniprot.org/core/author"Schneider-Poetsch H.A."xsd:string
http://purl.uniprot.org/citations/8000004http://purl.uniprot.org/core/author"Schneider-Poetsch H.A."xsd:string
http://purl.uniprot.org/citations/8000004http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8000004http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8000004http://purl.uniprot.org/core/name"Plant Mol. Biol."xsd:string
http://purl.uniprot.org/citations/8000004http://purl.uniprot.org/core/name"Plant Mol. Biol."xsd:string
http://purl.uniprot.org/citations/8000004http://purl.uniprot.org/core/pages"909-921"xsd:string
http://purl.uniprot.org/citations/8000004http://purl.uniprot.org/core/pages"909-921"xsd:string
http://purl.uniprot.org/citations/8000004http://purl.uniprot.org/core/title"Avenacosidase from oat: purification, sequence analysis and biochemical characterization of a new member of the BGA family of beta-glucosidases."xsd:string
http://purl.uniprot.org/citations/8000004http://purl.uniprot.org/core/title"Avenacosidase from oat: purification, sequence analysis and biochemical characterization of a new member of the BGA family of beta-glucosidases."xsd:string
http://purl.uniprot.org/citations/8000004http://purl.uniprot.org/core/volume"26"xsd:string
http://purl.uniprot.org/citations/8000004http://purl.uniprot.org/core/volume"26"xsd:string
http://purl.uniprot.org/citations/8000004http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8000004