http://purl.uniprot.org/citations/2361960 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/2361960 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/2361960 | http://www.w3.org/2000/01/rdf-schema#comment | "The complete peptide map of purified recombinant human interleukin 5 (rhIL-5) was determined to verify its primary structure, glycosylation sites, and disulfide bonding structure. Each peptide fragment generated by Achromobacter protease I (API) digestion was purified and characterized by amino acid analysis and amino acid sequence analysis. After digestion with API, we could identify all the peptides which were expected from human IL-5 cDNA sequence. The analyses of sulfhydryl content in rhIL-5 molecule and disulfide-containing peptide obtained from API digestion indicated that active form of rhIL-5 existed as an antiparallel dimer linked by two pairs of Cys-44 and Cys-86. In addition, we concluded that Thr-3 and Asn-28 were glycosylated. The results indicate that primary structure of rhIL-5 is highly homogeneous and observed heterogeneity is due to the difference in the content of carbohydrate."xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.org/dc/terms/identifier | "doi:10.1093/oxfordjournals.jbchem.a123041"xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.org/dc/terms/identifier | "doi:10.1093/oxfordjournals.jbchem.a123041"xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/author | "Tanaka S."xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/author | "Tanaka S."xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/author | "Adachi H."xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/author | "Adachi H."xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/author | "Katayama T."xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/author | "Katayama T."xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/author | "Tsujimoto M."xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/author | "Tsujimoto M."xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/author | "Kodama S."xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/author | "Kodama S."xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/author | "Minamitake Y."xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/author | "Minamitake Y."xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/name | "J. Biochem."xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/name | "J. Biochem."xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/pages | "292-297"xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/pages | "292-297"xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/title | "Structure of recombinant human interleukin 5 produced by Chinese hamster ovary cells."xsd:string |
http://purl.uniprot.org/citations/2361960 | http://purl.uniprot.org/core/title | "Structure of recombinant human interleukin 5 produced by Chinese hamster ovary cells."xsd:string |