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- W2028757538 abstract "A novel, highly specific protein modification approach is described. By using conventional molecular cloning techniques, a protein can be constructed and expressed such that the N-terminal residue is replaced by cysteine. Its 1,2-aminothiol structure reacts very specifically with a glyoxylyl group at pH 7 or below, forming a relatively stable thiazolidine bridge. Therefore, a glyoxylyl-based labeling agent (e.g., radioactive tags, fluorescent probes, biotin) can be used to specifically modify a protein at its N-terminus. To highlight this novel approach, a recombinant anti-insulin single chain antibody (scFv) was specifically biotinylated at its N-terminus even in the presence of other proteins in the total cell lysate. The glyoxylyl-biotinylated scFv retained binding activity similar to unmodified scFv." @default.
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- W2028757538 date "1999-04-24" @default.
- W2028757538 modified "2023-10-15" @default.
- W2028757538 title "Site-Specific Modification of a Single-Chain Antibody Using a Novel Glyoxylyl-Based Labeling Reagent" @default.
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- W2028757538 doi "https://doi.org/10.1021/bc980120k" @default.
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