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http://purl.uniprot.org/citations/10866809http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10866809http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10866809http://www.w3.org/2000/01/rdf-schema#comment"A cDNA clone, 1.8 kb long, was isolated from a venom gland cDNA library of Agkistrodon blomhoffi that encodes a large plurifunctional precursor composed of 263 amino-acid residues. Nucleotide sequence analysis of this clone revealed that sequences which code for blomhotin and a novel peptide Leu3-blomhotin are located in the N-terminal region of the precursor polypeptide, followed by four tandemly aligned sequences which code for three types of bradykinin-potentiating peptide. In the C-terminal region, the sequence for the C-type natriuretic peptide was located along with a preceding processing signal. The deduced amino-acid sequences for the four bradykinin-potentiating peptides coincided exactly with previously known sequences for potentiator B, potentiator C and potentiator E. The actual Leu3-blomhotin peptide was subsequently isolated from the venom of A. blomhoffi and characterized. Leu3-blomhotin possesses contractile activity in isolated rat stomach fundus smooth muscle in the same manner as blomhotin. Furthermore, it was shown that blomhotin and Leu3-blomhotin retained activity to inhibit the angiotensin-converting enzyme."xsd:string
http://purl.uniprot.org/citations/10866809http://purl.org/dc/terms/identifier"doi:10.1046/j.1432-1327.2000.01443.x"xsd:string
http://purl.uniprot.org/citations/10866809http://purl.org/dc/terms/identifier"doi:10.1046/j.1432-1327.2000.01443.x"xsd:string
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/author"Fujita Y."xsd:string
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/author"Fujita Y."xsd:string
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/author"Higuchi S."xsd:string
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/author"Higuchi S."xsd:string
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/author"Murayama N."xsd:string
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/author"Murayama N."xsd:string
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/author"Samejima Y."xsd:string
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/author"Samejima Y."xsd:string
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/author"Yanoshita R."xsd:string
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/author"Yanoshita R."xsd:string
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/author"Ohi H."xsd:string
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/author"Ohi H."xsd:string
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/author"Michel G.H."xsd:string
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/author"Michel G.H."xsd:string
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/author"Saguchi K."xsd:string
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/author"Saguchi K."xsd:string
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/10866809http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string