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http://purl.uniprot.org/citations/7579169http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7579169http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7579169http://www.w3.org/2000/01/rdf-schema#comment"Vacuolar processing enzymes (VPEs) are responsible for the maturation of seed proteins. These processing enzymes belong to a novel group of cysteine proteinases with molecular masses of 37 to 39 kDa. We isolated two genes of VPEs from a genomic library of Arabidopsis. The gene products were designated alpha-VPE and beta-VPE, and they were 56% identical in terms of amino acid sequence. The amino acid sequences of alpha-VPE and beta-VPE were also 55% and 67% identical to that of castor bean VPE, respectively. The gene for alpha-VPE had 7 introns, while that of beta-VPE had 8 introns. Northern blot analysis revealed that alpha-VPE is expressed in rosette leaves, cauline leaves and stems of Arabidopsis, while beta-VPE is predominantly expressed in the flowers and buds. Neither alpha-VPE nor beta-VPE is expressed in the siliques. This result strongly suggests that the isolated genes encode isozymes of VPE that are specific to vegetative organs."xsd:string
http://purl.uniprot.org/citations/7579169http://purl.org/dc/terms/identifier"doi:10.1007/bf00019120"xsd:string
http://purl.uniprot.org/citations/7579169http://purl.org/dc/terms/identifier"doi:10.1007/bf00019120"xsd:string
http://purl.uniprot.org/citations/7579169http://purl.uniprot.org/core/author"Hara-Nishimura I."xsd:string
http://purl.uniprot.org/citations/7579169http://purl.uniprot.org/core/author"Hara-Nishimura I."xsd:string
http://purl.uniprot.org/citations/7579169http://purl.uniprot.org/core/author"Nishimura M."xsd:string
http://purl.uniprot.org/citations/7579169http://purl.uniprot.org/core/author"Nishimura M."xsd:string
http://purl.uniprot.org/citations/7579169http://purl.uniprot.org/core/author"Kinoshita T."xsd:string
http://purl.uniprot.org/citations/7579169http://purl.uniprot.org/core/author"Kinoshita T."xsd:string
http://purl.uniprot.org/citations/7579169http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7579169http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7579169http://purl.uniprot.org/core/name"Plant Mol. Biol."xsd:string
http://purl.uniprot.org/citations/7579169http://purl.uniprot.org/core/name"Plant Mol. Biol."xsd:string
http://purl.uniprot.org/citations/7579169http://purl.uniprot.org/core/pages"81-89"xsd:string
http://purl.uniprot.org/citations/7579169http://purl.uniprot.org/core/pages"81-89"xsd:string
http://purl.uniprot.org/citations/7579169http://purl.uniprot.org/core/title"Homologues of a vacuolar processing enzyme that are expressed in different organs in Arabidopsis thaliana."xsd:string
http://purl.uniprot.org/citations/7579169http://purl.uniprot.org/core/title"Homologues of a vacuolar processing enzyme that are expressed in different organs in Arabidopsis thaliana."xsd:string
http://purl.uniprot.org/citations/7579169http://purl.uniprot.org/core/volume"29"xsd:string
http://purl.uniprot.org/citations/7579169http://purl.uniprot.org/core/volume"29"xsd:string
http://purl.uniprot.org/citations/7579169http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7579169
http://purl.uniprot.org/citations/7579169http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7579169
http://purl.uniprot.org/citations/7579169http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7579169
http://purl.uniprot.org/citations/7579169http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7579169