The FASEB Journal · 2001 · 25 citations · 59 references
PharmacyBiochemistryMolecular BiologyAntibody EngineeringEnzyme MechanismEnzymologyAntibody Library ConstructionCatalytic MechanismsEnzyme DiscoveryEnzyme-substrate RecognitionSubstrate SpecificityAmidase-mediated ActivationBeta-lactamase GenesCatalytic EfficiencyCatalytic SpecificityEnzyme Library ConstructionHeavy Chain StructureSequence HomologySequence Homology Detection
ABSTRACT A monoclonal antibody 9G4H9 that exhib¬its a β‐lactamase‐like activity was previously obtained in accordance with the idiotypic network theory. This abzyme presents the most catalytic efficiency in amidase activity described in literature (k cat = 0.9 mín −1 ). Some reports have demonstrated that functionality as complex as catalysis may be mimicked in this way. Comparison of the catalytic properties of both enzyme and abzyme previously allowed us to obtain better knowledge about 9G4H9 abzymatic machinery. In attempt to characterize this abzyme, the variable regions of kappa and heavy chain were cloned. We present a ‘universal’ method to clone the correct VΚ gene to bypass aberrant VΚ ( ab VΚ) produced by MOPC‐21‐derived hybridomas. Sequences obtained are compared in the GenBank database. The VH and VΚ genes present some important sequence homology with autoantibodies suggesting a direct relationship between catalytic anti‐idiotypic antibody and autoimmunity.—Débat, H., Avalle, B, Chose, O., Sarde, C.‐O., Friboulet, A., Thomas, D. Overpassing an aberrant VΚ gene to sequence an anti‐idiotypic abzyme with β‐lactamase‐like activity that could have a linkage with autoimmune dis¬eases. FASEB J. 15, 815‐822 (2001)
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Julie Thompson, Desmond G. Higgins, Toby J. Gibson · Nucleic Acids Research · 1994 · 64.9K citations · Full text
Michael A. Frohman, Michael Dush, Gail R. Martin · Proceedings of the National Academy of Sciences · 1988 · 4.6K citations · Full text