Structural characterization and interaction with RCA120 of a highly sulfated keratan sulfate from blue shark (Prionace glauca) cartilage
AuthorLi, Q.; Li, G.; Zhao, X.; Shan, X.; Cai, C.; Zhao, J.; Zhang, F.; Linhardt, Robert J.; Yu, G.
SubjectBiology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
Full CitationStructural characterization and interaction with RCA120 of a highly sulfated keratan sulfate from blue shark (Prionace glauca) cartilage, Q. Li, G. Li, X.Zhao, X. Shan, C. Cai, J. Zhao, F. Zhang, R. J. Linhardt, G. Yu, Marine Drugs, 16, 128, 2018.
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AbstractAs an important glycosaminoglycan, keratan sulfate (KS) mainly exists in corneal and cartilage, possessing various biological activities. In this study, we purified KS from blue shark (Prionace glauca) cartilage and prepared KS oligosaccharides (KSO) through keratanase II-catalyzed hydrolysis. The structures of KS and KSO were characterized using multi-dimensional nuclear magnetic resonance (NMR) spectra and liquid chromatography-mass spectrometry (LC-MS). Shark cartilage KS was highly sulfated and modified with ~2.69% N-acetylneuraminic acid (NeuAc) through α(2,3)-linked to galactose. Additionally, KS exhibited binding affinity to Ricinus communis agglutinin I (RCA120) in a concentration-dependent manner, a highly toxic lectin from beans of the castor plant. Furthermore, KSO from dp2 to dp8 bound to RCA120 in the increasing trend while the binding affinity of dp8 was superior to polysaccharide. These results define novel structural features for KS from Prionace glauca cartilage and demonstrate the potential application on ricin-antidote exploitation.;
DescriptionMarine Drugs, 16, 128; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
DepartmentThe Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
PublisherMultidisciplinary Digital Publishing Institute (MDPI)
RelationshipsThe Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; https://harc.rpi.edu/;
AccessCC BY — Creative Commons Attribution; Open Access; A full text version is available in DSpace@RPI;
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