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http://purl.uniprot.org/citations/16668896http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16668896http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16668896http://www.w3.org/2000/01/rdf-schema#comment"We purified and partially sequenced a purple (lambda(max) = 556 nanometers) acid phosphatase (APase; EC 3.1.3.2) secreted by soybean (Glycine max) suspension-culture cells. The enzyme is a metalloprotein with a Mn(2+) cofactor. This APase appears to be a glycoprotein with a monomer subunit molecular weight of 58,000 and an active dimer molecular weight of approximately 130,000. The protein has an isoelectric point of about 5.0 and a broad pH optimum centered near 5.5. The purified enzyme, assayed with p-nitrophenyl phosphate as the substrate, has a specific activity of 512 units per milligram protein and a K(m) of approximately 0.3 millimolar; phosphate is a competitive inhibitor with a K(i) of 0.7 millimolar. This APase is similar to one found in soybean seed meal but dissimilar to that found in soybean seedlings."xsd:string
http://purl.uniprot.org/citations/16668896http://purl.org/dc/terms/identifier"doi:10.1104/pp.99.2.391"xsd:string
http://purl.uniprot.org/citations/16668896http://purl.org/dc/terms/identifier"doi:10.1104/pp.99.2.391"xsd:string
http://purl.uniprot.org/citations/16668896http://purl.uniprot.org/core/author"McKnight T.D."xsd:string
http://purl.uniprot.org/citations/16668896http://purl.uniprot.org/core/author"McKnight T.D."xsd:string
http://purl.uniprot.org/citations/16668896http://purl.uniprot.org/core/author"Griffing L.R."xsd:string
http://purl.uniprot.org/citations/16668896http://purl.uniprot.org/core/author"Griffing L.R."xsd:string
http://purl.uniprot.org/citations/16668896http://purl.uniprot.org/core/author"Lebansky B.R."xsd:string
http://purl.uniprot.org/citations/16668896http://purl.uniprot.org/core/author"Lebansky B.R."xsd:string
http://purl.uniprot.org/citations/16668896http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/16668896http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/16668896http://purl.uniprot.org/core/name"Plant Physiol."xsd:string
http://purl.uniprot.org/citations/16668896http://purl.uniprot.org/core/name"Plant Physiol."xsd:string
http://purl.uniprot.org/citations/16668896http://purl.uniprot.org/core/pages"391-395"xsd:string
http://purl.uniprot.org/citations/16668896http://purl.uniprot.org/core/pages"391-395"xsd:string
http://purl.uniprot.org/citations/16668896http://purl.uniprot.org/core/title"Purification and characterization of a secreted purple phosphatase from soybean suspension cultures."xsd:string
http://purl.uniprot.org/citations/16668896http://purl.uniprot.org/core/title"Purification and characterization of a secreted purple phosphatase from soybean suspension cultures."xsd:string
http://purl.uniprot.org/citations/16668896http://purl.uniprot.org/core/volume"99"xsd:string
http://purl.uniprot.org/citations/16668896http://purl.uniprot.org/core/volume"99"xsd:string
http://purl.uniprot.org/citations/16668896http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16668896
http://purl.uniprot.org/citations/16668896http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16668896
http://purl.uniprot.org/citations/16668896http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16668896
http://purl.uniprot.org/citations/16668896http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16668896