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Characterization of specific sites on the Rubisco molecule recognized by monoclonal antibodies



Characterization of specific sites on the Rubisco molecule recognized by monoclonal antibodies



Plant Physiology & Biochemistry 35(7): 513-521



Four monoclonal antibodies (Mabs) against Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase, EC 4.1.1.39) from Hordeum vulgare L., previously described as inhibiting the enzyme activity, were characterized in respect to their effect on the active site of the enzyme. Two of the Mabs partially prevent Rubisco carbamylation in trapping experiments measuring the amount of 14CO-2 bound to Rubisco which was rendered non-exchangeable by 2-carboxyarabinitol-1,5-bisphosphate (CABP). Changes in the binding of the same Mabs to Rubisco complexed with some effectors: ribulose-1,5-bisphosphate (RuBP), phosphoenol pyruvate (PEP), fructose-1,6-bisphosphate (FBP), 6-phosphogluconate (6PG), were observed in inhibition ELISA reflecting affinity alteration. A reduced interaction with the complex of activated Rubisco with CABP was revealed for all the Mabs. Although none of the Mabs affect directly the activation or the substrate binding site of the enzyme, Mab affinity for Rubisco is dependent on Rubisco conformation. Sandwich ELISA experiments using Mabs and Rubisco with active site blocked by CABP, effectors bound to a putative regulatory site support the hypothesis about the existence of an allosteric site on the Rubisco molecule related with the enzyme regulation.

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