Binding of purified C1 subcomponents, C1 inactivator and their complexes to immobilized heparin.
Under specified conditions purified C1q, activated C1r and C1s and C1r-C1s complexes were bound independently of Ca2+, to heparin-Sepharose, and could be eluted by an increasing salt gradient. Zymogen C1r and C1s, C1r-C1s complexes, C1 inactivator, and C1r-C1s-C1 activator complexes were not bound. However, at lower conductance Ca2+ independent binding of C14 occurred, which was utilized in the purification of C14 and C1s. In the presence of C1t (serum amyloid P component), C1s was firmly retained on heparin-Sepharose, which was probably due to formation of a C1s-C1t complex.
D000682:Amyloid / Q000494:pharmacology; D002118:Calcium; D002846:Chromatography, Affinity; D003166:Complement Activating Enzymes / Q000378:metabolism*; D003174:Complement C1 Inactivator Proteins / Q000378:metabolism*; D015923:Complement C1r; D003173:Complement C1s; D006493:Heparin / Q000378:metabolism*; D006801:Humans; D012685:Sepharose; D000683:Serum Amyloid P-Component
D000682:Amyloid; D003174:Complement C1 Inactivator Proteins; D000683:Serum Amyloid P-Component; D006493:Heparin; D012685:Sepharose; D003166:Complement Activating Enzymes; D015923:Complement C1r; D003173:Complement C1s; D002118:Calcium