RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/10050046http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10050046http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10050046http://www.w3.org/2000/01/rdf-schema#comment"We previously identified the 26/29-kDa proteinase in the hemocytes of Sarcophaga peregrina (flesh fly) that appears to participate in elimination of foreign proteins in this insect [Eur. J. Biochem. 209, 939-944 (1992)]. Here, we report the cDNA cloning of this proteinase. The cDNA encodes a protein which includes both the 26- and 29-kDa subunit, strongly suggesting that the both subunits are derived from a single precursor protein. The 26- and 29-kDa subunit located at the amino-terminal and carboxyl-terminal of the precursor protein. The 29-kDa subunit itself appeared to be a proteinase, for this subunit had 52% sequence identity with Sarcophaga cathepsin L, while 26-kDa subunit had no significant similarity. We also showed that 26/29-kDa proteinase was insensitive to specific inhibitors of cathepsin L. These results indicate that this proteinase is a novel member of the papain family. We isolated similar cDNAs from Drosophila melanogaster and Periplaneta americana (cockroach), suggesting that this proteinase is conserved in a wide variety of insects and participates in their defense mechanisms."xsd:string
http://purl.uniprot.org/citations/10050046http://purl.org/dc/terms/identifier"doi:10.1093/oxfordjournals.jbchem.a022322"xsd:string
http://purl.uniprot.org/citations/10050046http://purl.uniprot.org/core/author"Kobayashi A."xsd:string
http://purl.uniprot.org/citations/10050046http://purl.uniprot.org/core/author"Kobayashi A."xsd:string
http://purl.uniprot.org/citations/10050046http://purl.uniprot.org/core/author"Natori S."xsd:string
http://purl.uniprot.org/citations/10050046http://purl.uniprot.org/core/author"Natori S."xsd:string
http://purl.uniprot.org/citations/10050046http://purl.uniprot.org/core/author"Fujimoto Y."xsd:string
http://purl.uniprot.org/citations/10050046http://purl.uniprot.org/core/author"Fujimoto Y."xsd:string
http://purl.uniprot.org/citations/10050046http://purl.uniprot.org/core/author"Kurata S."xsd:string
http://purl.uniprot.org/citations/10050046http://purl.uniprot.org/core/author"Kurata S."xsd:string
http://purl.uniprot.org/citations/10050046http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10050046http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10050046http://purl.uniprot.org/core/name"J. Biochem."xsd:string
http://purl.uniprot.org/citations/10050046http://purl.uniprot.org/core/name"J Biochem"xsd:string
http://purl.uniprot.org/citations/10050046http://purl.uniprot.org/core/pages"566-573"xsd:string
http://purl.uniprot.org/citations/10050046http://purl.uniprot.org/core/pages"566-573"xsd:string
http://purl.uniprot.org/citations/10050046http://purl.uniprot.org/core/title"Two subunits of the insect 26/29-kDa proteinase are probably derived from a common precursor protein."xsd:string
http://purl.uniprot.org/citations/10050046http://purl.uniprot.org/core/title"Two subunits of the insect 26/29-kDa proteinase are probably derived from a common precursor protein."xsd:string
http://purl.uniprot.org/citations/10050046http://purl.uniprot.org/core/volume"125"xsd:string
http://purl.uniprot.org/citations/10050046http://purl.uniprot.org/core/volume"125"xsd:string
http://purl.uniprot.org/citations/10050046http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10050046
http://purl.uniprot.org/citations/10050046http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10050046
http://purl.uniprot.org/citations/10050046http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10050046