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http://purl.uniprot.org/citations/10366732http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10366732http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10366732http://www.w3.org/2000/01/rdf-schema#comment"The analysis of fibroin secretion-deficient 'naked-pupa' mutant silkworms has suggested that the disulfide linkage between heavy (H) and light (L) chains of fibroin, produced by the silkworm, Bombyx mori, is essential in its efficient large-scale secretion from the posterior silk gland cells. However, the site of disulfide-linkage between H- and L-chains has not been determined. In this study, cysteine residues involved in the single disulfide linkage between H- and L-chains were identified as the twentieth residue from the carboxyl terminus of H-chain (Cys-c20) and Cys-172 of L-chain by sequencing of genomic clones and peptide analysis. Furthermore, Cys-c4 (fourth residue from the carboxyl terminus) and Cys-c1 at the carboxyl terminus of H-chain were shown to form an intramolecular disulfide bond."xsd:string
http://purl.uniprot.org/citations/10366732http://purl.org/dc/terms/identifier"doi:10.1016/s0167-4838(99)00088-6"xsd:string
http://purl.uniprot.org/citations/10366732http://purl.org/dc/terms/identifier"doi:10.1016/s0167-4838(99)00088-6"xsd:string
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/author"Tanaka K."xsd:string
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/author"Tanaka K."xsd:string
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/author"Takagi T."xsd:string
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/author"Takagi T."xsd:string
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/author"Kikuchi A."xsd:string
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/author"Kikuchi A."xsd:string
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/author"Mizuno S."xsd:string
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/author"Mizuno S."xsd:string
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/author"Ohtomo K."xsd:string
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/author"Ohtomo K."xsd:string
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/author"Ishikura K."xsd:string
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/author"Ishikura K."xsd:string
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/author"Waga S."xsd:string
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/author"Waga S."xsd:string
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/author"Kajiyama N."xsd:string
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/author"Kajiyama N."xsd:string
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/10366732http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string