FEBS Letters | |
Purification of complement components by hydrophobic affinity chromatography on phenyl—Sepharose | |
Fontaine, M.1  Pruvost, L.1  Al Salihi, A.1  Ripoche, J.1  | |
[1] Inserm U-78, 543 Chemin de la Bretèque, F-76230 Bois-Guillaume, France | |
关键词: Complement components C5 and C3; Purification; Affinity chromatography; hydrophobic; Phenyl—Sepharose; Native C3; Separation of C5; EDTA; ethylene-diamine-tetraacetic acid; ϵACA; ϵ-amino-caproïc acid; SDS—PAGE; sodium dodecyl sulfate—polyacrylamide gel electrophoresis; | |
DOI : 10.1016/0014-5793(82)81342-2 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Human complement components C5 and C3 were purified with 41% and 20% yields, respectively, by euglobulin precipitation, DEAE—Sephacel ion-exchange chromatography and gel filtration. Phenyl—Sepharose chromatography allowed the complete separation of C3 and C5. C3 bound loosely on the resin whereas C5 bound firmly and was eluted with 50% glycerin solution. Gel filtration on Sephacryl S-300 allowed the depletion of C4bp and H that contaminated C5 preparations. Homogeneity of C5 and C3 preparations was demonstrated by SDS—PAGE and immunochemical analysis. C5 and C3 consisted of two chains (α, 110000; β, 75000) linked by disulfide bridges.
【 授权许可】
Unknown
【 预 览 】
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