{"_buckets": {"deposit": "5ec32768-14ad-4ff7-9891-0fba79348713"}, "_deposit": {"id": "4963", "owners": [], "pid": {"revision_id": 0, "type": "depid", "value": "4963"}, "status": "published"}, "_oai": {"id": "oai:teapot.lib.ocha.ac.jp:00004963"}, "item_12_biblio_info_8": {"attribute_name": "\u66f8\u8a8c\u60c5\u5831", "attribute_value_mlt": [{"bibliographicIssueDates": {"bibliographicIssueDate": "2009-02-21", "bibliographicIssueDateType": "Issued"}, "bibliographic_titles": [{"bibliographic_title": "Glycoconjugate Journal"}]}]}, "item_12_description_17": {"attribute_name": "\u30d5\u30a9\u30fc\u30de\u30c3\u30c8", "attribute_value_mlt": [{"subitem_description": "application/pdf", "subitem_description_type": "Other"}, {"subitem_description": "text/plain", "subitem_description_type": "Other"}, {"subitem_description": "application/pdf", "subitem_description_type": "Other"}]}, "item_12_description_46": {"attribute_name": "\u8cc7\u6e90\u30bf\u30a4\u30d7", "attribute_value_mlt": [{"subitem_description": "\u5b66\u8853\u96d1\u8a8c\u8ad6\u6587", "subitem_description_type": "Other"}]}, "item_12_description_6": {"attribute_name": "\u6284\u9332", "attribute_value_mlt": [{"subitem_description": "A proteoglycan (PG) monomer is a macromolecule consisting of one or more glycosaminoglycan (GAG) chains attached to a core protein. PGs have signaling roles and modulatory functions in the extracellular matrix and at the cell surface. To elucidate the functions of higher-order PG structures, pseudoPGs that imitate the PG structure were prepared to develop probes and affinity adsorbents. Poly-L-lysine (PLL) or polyacrylamide (PAA) was coupled with various GAGs, then biotinylated, and the remaining amino groups were blocked to obtain the pseudoPG probes, biotinyl PLL (BPL)- or PAA (BPA)-GAGs. Lactoferrin exhibited 30-times higher affinity toward BPL-heparin than the conventional single-strand probe, biotin-hydrazide-heparin.Heparin-PLL was immobilized on a formyl-Sepharose and compared with the Hep-Sepharose in which heparin was directly immobilized to amino-Sepharose. Screening for ligands in normal rat brain revealed several proteins that specifically bound to either of the two adsorbents, indicating that the heparin-binding proteins exhibit specific recognition depending on the higher-order structure of the PG.", "subitem_description_type": "Abstract"}]}, "item_12_description_7": {"attribute_name": "\u5185\u5bb9\u8a18\u8ff0", "attribute_value_mlt": [{"subitem_description": "online first / \u003cbr/\u003eReceived: 28 July 2008 / Revised: 30 September 2008 / Accepted: 8 December 2008 / Published online: 21 February 2009", "subitem_description_type": "Other"}, {"subitem_description": "The original publication is available at www.springerlink.com", "subitem_description_type": "Other"}]}, "item_12_publisher_36": {"attribute_name": "\u51fa\u7248\u8005", "attribute_value_mlt": [{"subitem_publisher": "Springer Netherlands"}]}, "item_12_relation_54": {"attribute_name": "\u7570\u7248\u3067\u3042\u308b", "attribute_value_mlt": [{"subitem_relation_type": 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