Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
In Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/;
Studies on the effect of calcium in interactions between heparin and heparin cofactor II using surface plasmon resonance, F. Zhang, Y. Wu, Q. Ma, D. Hoppensteadt, J. Fareed, R. J. Linhardt, Clinical and Applied Thrombosis/Hemostasis, 10, 249-257, 2004.
Heparin is the most acidic polysaccharide in the human body and as a result interacts with many cationic species, including ions and proteins, giving rise to myriad biologic activities. Heparin cofactor II (HCII) is a serine protease inhibitor that resembles antithrombin (ATIII) in its ability to be activated by heparin. The interaction of heparin with HCII has been the focus of many studies using affinity chromatography and fluorescence spectroscopy. In this study, surface plasmon resonance (SPR) spectroscopy was used to quantitatively measure the interaction of heparin and HCII using a heparin biochip prepared by covalently immobilizing preformed albumin-heparin conjugate. HCII contains multiple EF hand domains that represent putative calcium ion binding sites. The interactions of HCII with heparin, low-molecular-weight heparin, and heparin oligosaccharides (disaccharide, tetrasaccharide, hexasaccharide) were examined in solution competition experiments using SPR. The results also showed while calcium ions enhanced the heparin/HCII interaction, the activity of heparin-HCII complex against thrombin was not calcium dependent but can be enhanced by the presence of calcium.;
Clinical and Applied Thrombosis/Hemostasis, 10, 249-257; 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.
The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Clinical and Applied Thrombosis/Hemostasis; https://harc.rpi.edu/;