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http://purl.uniprot.org/citations/2503378http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2503378http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2503378http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/2503378http://www.w3.org/2000/01/rdf-schema#comment"A heat-stable aminopeptidase with an N-terminal Ala-Pro-Asp-Ile-Pro-Leu sequence has been purified from Streptomyces griseus by heat treatment followed by gel-exclusion and anion-exchange chromatographic procedures. The enzyme is a monomeric zinc metalloenzyme showing an apparent molecular mass of 33 kDa by sodium dodecyl sulfate/polyacrylamide gel electrophoresis and 21 kDa by gel filtration on Superose 12. Calcium ions bind to the enzyme, pKCa 4.5, and activate it about sixfold when the substrate is leucine-4-nitroanilide (0.4 mM in 50 mM Tris/HCl pH 8.0, 25 degrees C). Binding of Ca2+ also contributes to the thermal stability of the protein. This aminopeptidase may be useful for two-stage assays of bacterial and mammalian metalloendopeptidases; it may also serve in studies of proteolytic enzyme activation by calcium ions."xsd:string
http://purl.uniprot.org/citations/2503378http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/2503378http://purl.uniprot.org/core/name"Eur. J. Biochem."xsd:string
http://purl.uniprot.org/citations/2503378http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1989.tb14952.x"xsd:string
http://purl.uniprot.org/citations/2503378http://purl.org/dc/terms/identifier"doi:10.1111/j.1432-1033.1989.tb14952.x"xsd:string
http://purl.uniprot.org/citations/2503378http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2503378
http://purl.uniprot.org/citations/2503378http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2503378
http://purl.uniprot.org/citations/2503378http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2503378
http://purl.uniprot.org/citations/2503378http://purl.uniprot.org/core/author"Blumberg S."xsd:string
http://purl.uniprot.org/citations/2503378http://purl.uniprot.org/core/author"Blumberg S."xsd:string
http://purl.uniprot.org/citations/2503378http://purl.uniprot.org/core/author"Spungin A."xsd:string
http://purl.uniprot.org/citations/2503378http://purl.uniprot.org/core/author"Spungin A."xsd:string
http://purl.uniprot.org/citations/2503378http://purl.uniprot.org/core/date"1989"xsd:gYear
http://purl.uniprot.org/citations/2503378http://purl.uniprot.org/core/date"1989"xsd:gYear
http://purl.uniprot.org/citations/2503378http://purl.uniprot.org/core/pages"471-477"xsd:string
http://purl.uniprot.org/citations/2503378http://purl.uniprot.org/core/pages"471-477"xsd:string
http://purl.uniprot.org/citations/2503378http://purl.uniprot.org/core/title"Streptomyces griseus aminopeptidase is a calcium-activated zinc metalloprotein. Purification and properties of the enzyme."xsd:string
http://purl.uniprot.org/citations/2503378http://purl.uniprot.org/core/title"Streptomyces griseus aminopeptidase is a calcium-activated zinc metalloprotein. Purification and properties of the enzyme."xsd:string
http://purl.uniprot.org/citations/2503378http://purl.uniprot.org/core/volume"183"xsd:string
http://purl.uniprot.org/citations/2503378http://purl.uniprot.org/core/volume"183"xsd:string
http://purl.uniprot.org/citations/2503378http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/2503378
http://purl.uniprot.org/citations/2503378http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/2503378