Purification of colony-stimulating factor by affinity chromatography
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چکیده
منابع مشابه
Purification by Affinity Chromatography
The glycine receptor of rat spinal cord was solubilized with the nonionic detergent Triton X-100 and subsequently purified by affinity chromatography on aminostrychnine-agarose and wheat germ agglutininSepharose. An overall purification of 1950-fold was achieved. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and mercaptoethano1 revealed three glycine receptor-asso...
متن کاملFractionation of antibodies to L-cell colony-stimulating factor by affinity chromatography.
Purified L-cell colony-stimulating factor (CSF) was coupled to cyanogen-bromide-activated Sepharose and used to selectively fractionate antibodies to this factor. With the use of a simplified two-step washing and elution technique, there was 50%--70% binding of the anti-CSF, with recovery of 60%--100% of the bound material. Both the native antiserum and purified anti-CSF fractions were inhibit...
متن کاملProtein Purification by Affinity Chromatography
The preparation of a number of agarose and polyacrylamide bead derivatives useful in the purification of proteins by afhnity chromatography is described. These techniques permit (a) the attachment of ligands to the gel through extended hydrocarbon chains which place the ligand at varying distances from the gel matrix backbone; (b) the covalent attachment of ligands to agarose or polyacrylamide ...
متن کاملProtein Purification by Affinity Chromatography
The preparation of a number of agarose and polyacrylamide bead derivatives useful in the purification of proteins by afhnity chromatography is described. These techniques permit (a) the attachment of ligands to the gel through extended hydrocarbon chains which place the ligand at varying distances from the gel matrix backbone; (b) the covalent attachment of ligands to agarose or polyacrylamide ...
متن کاملPurification of cartilage-derived growth factor by heparin affinity chromatography.
Cartilage-derived growth factor (CDGF) was found to bind tightly to columns of immobilized heparin and could be eluted with concentrations of salt in the order of 1.6-1.8 M NaCl. The molecular weight of CDGF was estimated to be 18,000-20,000 by high performance liquid-size exclusion chromatography. The affinity of CDGF for heparin greatly facilitated its purification. Highly purified CDGF activ...
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ژورنال
عنوان ژورنال: Blood
سال: 1982
ISSN: 0006-4971,1528-0020
DOI: 10.1182/blood.v60.1.238.238