The C-terminus type I collagen is a major binding site for heparin |
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| Affiliation: | 1. Department of Chemistry, Manipal Institute of Technology, Manipal Academy of Higher Education, Manipal, Karnataka 576104, India;2. Department of Chemistry, University of Munich (LMU), Butenandtstraβe 5-13, (D), 81377 Munich, Germany;1. Key Laboratory of Geographic Information Science (Ministry of Education), East China Normal University, Shanghai 200241, China;2. School of Geographic Sciences, East China Normal University, Shanghai 200241, China;3. Shanghai Key Laboratory for Urban Ecological Processes and Eco-Restoration, East China Normal University, Shanghai 200241, China;4. Department of Environmental Science, East China Normal University, No. 500, Dongchuan Road, Minhang District, Shanghai, China;5. Department of Geography and Planning, The University of Toledo, Toledo 43606, United States;1. Department of Chemical Engineering, Landmark University, P.M.B. 1001, Omu-Aran, Kwara State, Nigeria;2. Department of Chemical Engineering, University of Ilorin, P.M.B. 1515, Ilorin, Kwara State, Nigeria;1. Bioengineering and Nanomedicine Group, Faculty of Medicine and Health Technologies, Tampere University, 33720 Tampere, Finland;2. Department of Bioengineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan;3. Cellular and Molecular Biotechnology Research Institute (CMB), National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central Fifth, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8565, Japan;4. H5 Department of Laboratory Medicine, Karolinska Institute, Stockholm, Sweden;5. Department of Immunology, Genetics and Pathology, Rudbeck Laboratory, Uppsala University, SE-75105, Sweden;6. Macromolecular Chemistry, Department of Chemistry - Ångström Laboratory, Uppsala University, 751 21 Uppsala, Sweden |
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| Abstract: | The binding of collagens and fragments of type I collagen to heparin was studied by gel electrophoresis and affinity chromatography. Samples bound in 150 mM NaCl/10 mM Hepes (pH6.5) were eluted with 2 M NaCl, 6 M urea, or a linear gradient of 0.15–1.0 M NaCl. The triple-helical conformation was shown to be essential for binding. The vertebrate collagenase-generated C-terminal fragment, TCB was shown to have greater binding affinity for heparin than the N-terminal TCA fragment. Both type II collagen and the NC1 domain of type IV collagen bound to heparin, whereas pepsin-solubilized tetrameric type IV failed to bind. |
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