Abstract
It has been proposed that the function of serum amyloid P component (SAP) may closely relate with its binding to polysaccharides, especially glycosaminoglycans. We employed a quantitative immunoelectrophoresis (QIE) method and a native polyacrylamide gel electrophoresis (PAGE) method to characterize the SAP-heparin binding in soluble state. The SAP-heparin binding showed positive cooperativity. The apparent numbers of heparin molecules bound to SAP varied with the calcium concentration with a ratio of 1:1 (SAP/heparin), a Kd of 2.06·10-7 M at 0.1 mM CaCl2 and a ratio of 1:1.6 (SAP/heparin), a Kd of 3.91·10-7 M at 2 mM CaCl2, when estimated by the QIE method. No binding between SAP and heparin was observed in the absence of calcium. Magnesium and barium failed to induce the formation of SAP-heparin complex. Furthermore, they showed inhibitory effects on the calcium-mediated complex formation. We propose that heparin might be a regular to modulate the anticoagulant activity of SAP and a useful drug to prevent SAP deposition on amyloid deposits.
Original language | English |
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Pages (from-to) | 143-148 |
Number of pages | 6 |
Journal | Biochimica et Biophysica Acta - General Subjects |
Volume | 1201 |
Issue number | 2 |
DOIs | |
State | Published - Nov 11 1994 |
Bibliographical note
Funding Information:Abbreviations: SAP, serum amyloid P component; QIE, quantitative immunoelectrophoresis; PAGE, polyacrylamide gel electrophoresis; BSA, bovine serum albumin. * Corresponding author. Fax: +81 6 8727485. l Visiting scholar from Taishan Medical College, Taian, Shandong, China, financially supported by the Japan Health Science Foundation. 2 Visiting scholar from Taian Central Hospital, Taian, Shandong, China.
Keywords
- Amyloid P component
- Binding
- Glycosaminoglycan
- Heparin
- Serum
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology