By Meir Wilchek, Irwin Chaiken (auth.), Pascal Bailon, George K. Ehrlich, Wen-Jian Fung, Wolfgang Berthold (eds.)
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Additional resources for Affinity Chromatography: Methods and Protocols
The following method utilizes Protein G Sepharose as the support that has a more complete spectrum of binding affinities than Protein A Sepharose for monoclonal antibodies of murine and rat origin. The kinetics of the crosslinker concentration was studied in order to achieve near maximal binding capacity. The protocol is a laboratory-scale procedure designed to crosslink a specific immunoglobin G (IgG) to Protein G Sepharose at a density of 2 mg/mL. The two general steps in the immobilization of antibodies to Protein G Sepharose are (1) binding purified IgG to Protein G Sepharose and (2) incubating of the antibody-bound PGS with crosslinking reagent.
5. 2 M sodium chloride (see Note 8). Collect 1-min fractions. , Middletown, WI). 6. Reequilibrate the column with 5 cv of PBS. 7. Pool the protein fractions and determine the amount of protein in the eluate using Coomassie Plus Protein Assay (see Note 9). 3. Column Preparation Suspend the 120 mL of receptor–affinity adsorbent in 250 mL of PBS by stirring gently. Pour the slurry into the column. Add additional PBS, if there is less than 16 cm high of slurry in the column (see Note 10). Allow the adsorbent to settle for approx 15 min.
499, 235. 4. , and Olin, B. (1983) Immobilized metal ion affinity adsorption and immobilized metal ion affinity chromatography of biomaterials. Serum protein affinities for gel-immobilized iron and nickel ions. Biochemistry 22, 1621. 56 Schwarz 5. Hale, J. , and Beidler, D. E. (1994) Purification of humanized murine and murine monoclonal antibodies using immobilized metal-affinity chromatography. Anal. Biochem. 222, 29. 6. Al-Mashikhi, S. , and Nakai, S. (1988) Separation of immunoglobulins and lactoferrin from cheese whey by chelating chromatography.