@article{oai:teapot.lib.ocha.ac.jp:00004963,
 author = {Nakagawa, Keiko and Nakamura, Kosuke and Haishima, Yuji and Yamagami, Makiko and Saito, Kana and Sakagami, Hiromi and Ogawa, Haruko},
 journal = {Glycoconjugate Journal},
 month = {Feb},
 note = {application/pdf, text/plain, application/pdf, 学術雑誌論文, 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., online first / <br/>Received: 28 July 2008 / Revised: 30 September 2008 / Accepted: 8 December 2008 / Published online: 21 February 2009, The original publication is available at www.springerlink.com},
 title = {Pseudoproteoglycan (pseudoPG) probes that simulate PG macromolecular structure for screening and isolation of PG-binding proteins},
 year = {2009}
}