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http://purl.uniprot.org/citations/3263966http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3263966http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3263966http://www.w3.org/2000/01/rdf-schema#comment"A low molecular weight serine protease inhibitor, named trypstatin, was purified from rat peritoneal mast cells. It is a single polypeptide with 61 amino acid residues and an Mr of 6610. Trypstatin markedly inhibits blood coagulation factor Xa (Ki = 1.2 x 10(-10) M) and tryptase (Ki = 3.6 x 10(-10) M) from rat mast cells, which have activities that convert prothrombin to thrombin. It also inhibits porcine pancreatic trypsin (Ki = 1.4 x 10(-8) M) and chymase (Ki = 2.4 x 10(-8) M) from rat mast cells, but not papain, alpha-thrombin, or porcine pancreatic elastase. Trypstatin forms a complex in a molar ratio of 1:1 with trypsin and one subunit of tryptase. The complete amino acid sequence of this inhibitor was determined and compared with those of Kunitz-type inhibitors. Trypstatin has a high degree of sequence homology with human and bovine inter-alpha-trypsin inhibitors, A4(751) Alzheimer's disease amyloid protein precursor, and basic pancreatic trypsin inhibitor. However, unlike other known Kunitz-type protease inhibitors, it inhibits factor Xa most strongly."xsd:string
http://purl.uniprot.org/citations/3263966http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(19)81329-7"xsd:string
http://purl.uniprot.org/citations/3263966http://purl.org/dc/terms/identifier"doi:10.1016/s0021-9258(19)81329-7"xsd:string
http://purl.uniprot.org/citations/3263966http://purl.uniprot.org/core/author"Katunuma N."xsd:string
http://purl.uniprot.org/citations/3263966http://purl.uniprot.org/core/author"Katunuma N."xsd:string
http://purl.uniprot.org/citations/3263966http://purl.uniprot.org/core/author"Kido H."xsd:string
http://purl.uniprot.org/citations/3263966http://purl.uniprot.org/core/author"Kido H."xsd:string
http://purl.uniprot.org/citations/3263966http://purl.uniprot.org/core/author"Yokogoshi Y."xsd:string
http://purl.uniprot.org/citations/3263966http://purl.uniprot.org/core/author"Yokogoshi Y."xsd:string
http://purl.uniprot.org/citations/3263966http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/3263966http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/3263966http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/3263966http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/3263966http://purl.uniprot.org/core/pages"18104-18107"xsd:string
http://purl.uniprot.org/citations/3263966http://purl.uniprot.org/core/pages"18104-18107"xsd:string
http://purl.uniprot.org/citations/3263966http://purl.uniprot.org/core/title"Kunitz-type protease inhibitor found in rat mast cells. Purification, properties, and amino acid sequence."xsd:string
http://purl.uniprot.org/citations/3263966http://purl.uniprot.org/core/title"Kunitz-type protease inhibitor found in rat mast cells. Purification, properties, and amino acid sequence."xsd:string
http://purl.uniprot.org/citations/3263966http://purl.uniprot.org/core/volume"263"xsd:string
http://purl.uniprot.org/citations/3263966http://purl.uniprot.org/core/volume"263"xsd:string
http://purl.uniprot.org/citations/3263966http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3263966
http://purl.uniprot.org/citations/3263966http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3263966
http://purl.uniprot.org/citations/3263966http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/3263966
http://purl.uniprot.org/citations/3263966http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/3263966