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http://purl.uniprot.org/citations/6555050http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/6555050http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/6555050http://www.w3.org/2000/01/rdf-schema#comment"Proelastase has been purified to homogeneity from rat pancreatic tissue by a combination of CM-Sephadex and immobilized protease inhibitor affinity resins. Trypsin activation yields an elastolytic enzyme that possesses a specificity toward small hydrophobic residues in synthetic amide substrates, similar to those of porcine elastase 1 and canine elastase. However, the rat enzyme also rapidly hydrolyzes a substrate containing tyrosine in the P1 position. N-Terminal sequence analysis reveals that rat proelastase has an identical activation peptide with that of porcine proelastase 1 and has two conservative amino acid sequence differences from the activation peptide of canine proelastase. The sequence data established that rat proelastase corresponds to the elastase 1 mRNA clone isolated by MacDonald et al. [MacDonald, R. J., Swift, G. H., Quinto, C., Swain, W., Pictet, R. L., Nikovits, W., & Rutter, W. J. (1982) Biochemistry 21, 1453]. The sequence and substrate data obtained for rat and canine elastases suggest that there is a family of pancreatic elastases with properties similar to those of the classically described porcine elastase 1."xsd:string
http://purl.uniprot.org/citations/6555050http://purl.org/dc/terms/identifier"doi:10.1021/bi00285a008"xsd:string
http://purl.uniprot.org/citations/6555050http://purl.org/dc/terms/identifier"doi:10.1021/bi00285a008"xsd:string
http://purl.uniprot.org/citations/6555050http://purl.uniprot.org/core/author"Largman C."xsd:string
http://purl.uniprot.org/citations/6555050http://purl.uniprot.org/core/author"Largman C."xsd:string
http://purl.uniprot.org/citations/6555050http://purl.uniprot.org/core/date"1983"xsd:gYear
http://purl.uniprot.org/citations/6555050http://purl.uniprot.org/core/date"1983"xsd:gYear
http://purl.uniprot.org/citations/6555050http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/6555050http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/6555050http://purl.uniprot.org/core/pages"3763-3770"xsd:string
http://purl.uniprot.org/citations/6555050http://purl.uniprot.org/core/pages"3763-3770"xsd:string
http://purl.uniprot.org/citations/6555050http://purl.uniprot.org/core/title"Isolation and characterization of rat pancreatic elastase."xsd:string
http://purl.uniprot.org/citations/6555050http://purl.uniprot.org/core/title"Isolation and characterization of rat pancreatic elastase."xsd:string
http://purl.uniprot.org/citations/6555050http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/6555050http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/6555050http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/6555050
http://purl.uniprot.org/citations/6555050http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/6555050
http://purl.uniprot.org/citations/6555050http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/6555050
http://purl.uniprot.org/citations/6555050http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/6555050
http://purl.uniprot.org/uniprot/P00773http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/6555050
http://purl.uniprot.org/uniprot/#_kb.P00773_up.isolatedFrom_tissue.736http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/6555050
http://purl.uniprot.org/uniprot/P00773#attribution-8C9F5F1DA40F48BE2AF581206A4D12AFhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/6555050
http://purl.uniprot.org/uniprot/#_P00773-citation-6555050http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/6555050