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http://purl.uniprot.org/citations/1993171http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1993171http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1993171http://www.w3.org/2000/01/rdf-schema#comment"The disulfide pairings of mouse and human interleukin 4 (IL-4) proteins have been determined. The purified proteins, synthesized by recombinant DNA technology, are fully active as judged by their ability to stimulate an appropriate biological response in a variety of functional assays. Peptide maps were produced by digesting the proteins with pepsin and separating the resulting fragments by reverse-phase HPLC using linear acetonitrile-TFA gradients. Cystine-containing peptides were identified by determining which reverse-phase peaks showed an altered elution pattern after reduction. These peptides were purified further and defined by composition and sequence analysis. Three sets of disulfide-linked peptides were consistently identified for each protein. For mouse IL-4, the first and fifth, second and fourth, and third and sixth cysteines are joined. The disulfide bonds in human IL-4 are between the first and sixth, second and fourth, and third and fifth cysteines. A large double-loop region within the central three-fifths of each protein is stabilized by these bonds. Sequence analysis of the peptides containing the third and fifth cysteines of human IL-4 also demonstrated that only one of the potential N-glycosylation sites is used by C127 mammary tumor cells. Complete alkylation of mouse IL-4 under mild conditions completely destroyed its biological activity in a hematopoietic precursor cell proliferation assay."xsd:string
http://purl.uniprot.org/citations/1993171http://purl.org/dc/terms/identifier"doi:10.1021/bi00220a011"xsd:string
http://purl.uniprot.org/citations/1993171http://purl.org/dc/terms/identifier"doi:10.1021/bi00220a011"xsd:string
http://purl.uniprot.org/citations/1993171http://purl.uniprot.org/core/author"Carr C."xsd:string
http://purl.uniprot.org/citations/1993171http://purl.uniprot.org/core/author"Carr C."xsd:string
http://purl.uniprot.org/citations/1993171http://purl.uniprot.org/core/author"Kimack N.M."xsd:string
http://purl.uniprot.org/citations/1993171http://purl.uniprot.org/core/author"Kimack N.M."xsd:string
http://purl.uniprot.org/citations/1993171http://purl.uniprot.org/core/author"Aykent S."xsd:string
http://purl.uniprot.org/citations/1993171http://purl.uniprot.org/core/author"Aykent S."xsd:string
http://purl.uniprot.org/citations/1993171http://purl.uniprot.org/core/author"Levine A.D."xsd:string
http://purl.uniprot.org/citations/1993171http://purl.uniprot.org/core/author"Levine A.D."xsd:string
http://purl.uniprot.org/citations/1993171http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1993171http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1993171http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/1993171http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/1993171http://purl.uniprot.org/core/pages"1515-1523"xsd:string
http://purl.uniprot.org/citations/1993171http://purl.uniprot.org/core/pages"1515-1523"xsd:string
http://purl.uniprot.org/citations/1993171http://purl.uniprot.org/core/title"Disulfide assignments in recombinant mouse and human interleukin 4."xsd:string
http://purl.uniprot.org/citations/1993171http://purl.uniprot.org/core/title"Disulfide assignments in recombinant mouse and human interleukin 4."xsd:string
http://purl.uniprot.org/citations/1993171http://purl.uniprot.org/core/volume"30"xsd:string
http://purl.uniprot.org/citations/1993171http://purl.uniprot.org/core/volume"30"xsd:string
http://purl.uniprot.org/citations/1993171http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1993171
http://purl.uniprot.org/citations/1993171http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1993171