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<http://bio2rdf.org/drugbank:DB01271_nanopub.RAR3zwPuwmzZO0Z3xXrtTf6psll8i6rzNQpY4GV2AHXtI> <http://www.nanopub.org/nschema#hasProvenance> <http://bio2rdf.org/drugbank:DB01271_nanopub.RAR3zwPuwmzZO0Z3xXrtTf6psll8i6rzNQpY4GV2AHXtI#provenance> <http://bio2rdf.org/drugbank:DB01271_nanopub.RAR3zwPuwmzZO0Z3xXrtTf6psll8i6rzNQpY4GV2AHXtI#head> .
<http://bio2rdf.org/drugbank:DB01271_nanopub.RAR3zwPuwmzZO0Z3xXrtTf6psll8i6rzNQpY4GV2AHXtI> <http://www.nanopub.org/nschema#hasPublicationInfo> <http://bio2rdf.org/drugbank:DB01271_nanopub.RAR3zwPuwmzZO0Z3xXrtTf6psll8i6rzNQpY4GV2AHXtI#publicationInfo> <http://bio2rdf.org/drugbank:DB01271_nanopub.RAR3zwPuwmzZO0Z3xXrtTf6psll8i6rzNQpY4GV2AHXtI#head> .
<http://bio2rdf.org/drugbank:DB01271_nanopub.RAR3zwPuwmzZO0Z3xXrtTf6psll8i6rzNQpY4GV2AHXtI> <http://www.w3.org/1999/02/22-rdf-syntax-ns#type> <http://www.nanopub.org/nschema#Nanopublication> <http://bio2rdf.org/drugbank:DB01271_nanopub.RAR3zwPuwmzZO0Z3xXrtTf6psll8i6rzNQpY4GV2AHXtI#head> .
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<http://bio2rdf.org/drugbank:DB01271> <http://bio2rdf.org/bio2rdf_vocabulary:x-identifiers.org> <http://identifiers.org/drugbank/DB01271> <http://bio2rdf.org/drugbank:DB01271_nanopub.RAR3zwPuwmzZO0Z3xXrtTf6psll8i6rzNQpY4GV2AHXtI#assertion> .
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<http://bio2rdf.org/drugbank:DB01271> <http://bio2rdf.org/drugbank_vocabulary:x-atc> <http://bio2rdf.org/atc:A16AB09> <http://bio2rdf.org/drugbank:DB01271_nanopub.RAR3zwPuwmzZO0Z3xXrtTf6psll8i6rzNQpY4GV2AHXtI#assertion> .
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<http://bio2rdf.org/drugbank:DB01271> <http://purl.org/dc/terms/description> "Idursulfase is a purified form of human iduronate-2-sulfatase, a lysosomal enzyme. Idursulfase is produced by recombinant DNA technology in a human cell line. Idursulfase is an enzyme that hydrolyzes the 2-sulfate esters of terminal iduronate sulfate residues from the glycosaminoglycans dermatan sulfate and heparan sulfate in the lysosomes of various cell types. Idursulfase is a 525-amino acid glycoprotein with a molecular weight of approximately 76 kilodaltons. The enzyme contains eight asparagine-linked glycosylation sites occupied by complex oligosaccharide structures. The enzyme activity of idursulfase is dependent on the post-translational modification of a specific cysteine to formylglycine."@en <http://bio2rdf.org/drugbank:DB01271_nanopub.RAR3zwPuwmzZO0Z3xXrtTf6psll8i6rzNQpY4GV2AHXtI#assertion> .
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<http://download.bio2rdf.org/release/3/drugbank/drugbank.nq.gz> <http://purl.org/dc/terms/created> "2015-01-09T17:00:50-05:00"^^<http://www.w3.org/2001/XMLSchema#dateTime> <http://bio2rdf.org/drugbank:DB01271_nanopub.RAR3zwPuwmzZO0Z3xXrtTf6psll8i6rzNQpY4GV2AHXtI#provenance> .
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