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  • Title: Purification and application of a single-chain Fv antibody fragment specific to hepatitis B virus surface antigen.
    Author: Canaán-Haden L, Ayala M, Fernández-de-Cossio ME, Pedroso I, Rodés L, Gavilondo JV.
    Journal: Biotechniques; 1995 Oct; 19(4):606-8, 610, 612 passim. PubMed ID: 8777055.
    Abstract:
    Immobilized metal affinity chromatography (IMAC) has been recently applied to the purification of of recombinant proteins bearing multi-histidine domains at their N or C terminus. We have now used this procedure for the single-step purification of an anti-Hepatitis B virus surface antigen (HBsAg) single-chain Fv (scFv) antibody fragment. Adjusting the metal ion (Cu+2 or Ni+2) and elution conditions (pH or imidazole), we efficiently separated active scFv forms from inactive molecules. Achieved purity was 93%, with a 20% yield with respect to the scFv content in the initial material. The pure scFv was coupled to CNBr-activated Sepharose 4B and compared the original monoclonal antibody (MAb) CB-Hep.1 in the immunoaffinity purification of a vaccine recombinant HBsAg (r-HBsAg). Results indicate that eluted antigen per mg of coupled ligand was similar for the scFv and the MAb when pure r-HBsAg was used as starting material. Preliminary results with unpurified starting material are also encouraging.
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