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http://purl.uniprot.org/citations/1694763http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1694763http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1694763http://www.w3.org/2000/01/rdf-schema#comment"Rat hepatocytes have the potential to secrete three similar acidic glycoproteins, serine protease inhibitors 1, 2 and 3 (SPI-1, SPI-2, SPI-3), recognized by the same antibodies. They were synthesized as precursors of comparable sizes (45 kDa), which were post-translationally modified by N-glycosylation at three (SPI-3) or four (SPI-1 and SPI-2) sites. This appeared to account for the size difference of mature proteins. The mRNA sequences, derived from cDNA clones, displayed a high degree of similarity (70-90%), except the sequence of the antiprotease-reactive centers which were completely divergent. SPI-1 and SPI-2 mRNAs were of similar sizes (1.8 kb), and were smaller than that of SPI-3 (2.2 kb); the difference corresponded to a longer, 3'-end untranslated sequence. Production of SPI-1 and SPI-2, which was constitutive in the normal animal, could be abolished by hypophysectomy and was strongly decreased during acute inflammation. In contrast, production of SPI-3, which was barely detectable in normal rats, was transiently induced during inflammation."xsd:string
http://purl.uniprot.org/citations/1694763http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1990.tb15587.x"xsd:string
http://purl.uniprot.org/citations/1694763http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1990.tb15587.x"xsd:string
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/author"Pages G."xsd:string
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/author"Pages G."xsd:string
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/author"le Cam A."xsd:string
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/author"le Cam A."xsd:string
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/author"le Cam G."xsd:string
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/author"le Cam G."xsd:string
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/author"Mariller M."xsd:string
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/author"Mariller M."xsd:string
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/author"Rouayrenc J.F."xsd:string
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/author"Rouayrenc J.F."xsd:string
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/date"1990"xsd:gYear
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/pages"385-391"xsd:string
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/pages"385-391"xsd:string
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/title"Molecular characterization of three rat liver serine-protease inhibitors affected by inflammation and hypophysectomy. Protein and mRNA analysis and cDNA cloning."xsd:string
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/title"Molecular characterization of three rat liver serine-protease inhibitors affected by inflammation and hypophysectomy. Protein and mRNA analysis and cDNA cloning."xsd:string
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/volume"190"xsd:string
http://purl.uniprot.org/citations/1694763http://purl.uniprot.org/core/volume"190"xsd:string