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Small-angle x-ray scattering of high- and low-affinity heparin
Authors:B A Khorramian  S S Stivala
Institution:1. Department of Chemistry, Long Island University, Brooklyn, New York 11201, USA;2. Department of Chemistry and Chemical Engineering, Stevens Institute of Technology, Hoboken, New Jersey 07030 USA;1. Department of Chemistry, 578 S. Shaw Lane, Room 426, Michigan State University, East Lansing, MI 48824, USA;2. Department of Radiology, Michigan State University, East Lansing, MI 48824, USA;3. Department of Psychology, Michigan State University, East Lansing, MI 48824, USA;3. Institute for Protein Research, Osaka University, Yamadaoka 3-2, Suita, Osaka 565-0871, Japan;4. the Department of Biochemistry, Eötvös Loránd University, Pázmány sétány 1/C, Budapest 1117, Hungary;1. School of Materials Science and Engineering, Beijing Institute of Technology, Beijing, 100081, China;2. Beijing Key Laboratory of Construction Tailorable Advanced Functional Materials and Green Applications, Beijing, 100081, China
Abstract:Solution characterization of heparin with high affinity (HA) and low affinity (LA) for antithrombin III was performed using the methods of small-angle x-ray scattering (SAXS), viscometry, and aqueous gel permeation chromatography (GPC). SAXS provided various topological parameters including the radius of gyration (S2]1/2), radius of gyration of cross-section (S2]q1/2), persistence length (a*), contour length (L), and mass parameters, e.g., overall molecular mass (Mr), and mass per unit length (Mq). The molecular weights of HA and LA pig mucosal heparins were found to be 14,900 and 11,500 and the respective radii of gyration were 40.1 and 33.6 A. The persistence lengths of HA and LA were 21.3 and 20.3 A, respectively. These parameters were compared to SAXS data of heparin S. S. Stivala, M. Herbst, O. Kratky, and I. Pilz (1968) Arch. Biochem. Biophys. 127, 795-802] fractionated according to molecular weight only. It was found that the various experimental values of this heparin lie somewhere in between those of HA and LA heparins. It appears that there are no appreciable differences in the physico-chemical properties, including conformation, among the heparins in H2O at 25 degrees C.
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