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Biopolymers

Biopolymers

IF: 3.2
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β-Galactosidase: Immune recognition of conformation and mechanism of antibody-induced catalytic activation

Published:1 January 1983 DOI: 10.1002/bip.360220159
Franco Celada, Roberto Strom

Abstract

Activation of mutant β-galactosidase by antibodies can be explained by a “selection” mechanism in which the antibody binds and stabilizes those mutants in a native-like conformation and by an “induction” mechanism where binding of the antibody itself induces a conformational change activating β-galactosidase. The “selection” hypothesis was tested by passing β-galactosidase through a column packed with monoclonal antibody-derivatized Sepharose. The antibody retains the active, in preference to the inactive, proteins. The “induction” mechanism was tested by mixing antibody–Sepharose with mutant β-galactosidase and measuring enzyme activity before mixing and that remaining in the supernatant. The activity of the antibody–Sepharose pellet exceeded the sum of the original activity plus supernatant activity. As a result of these experiments, both mechanisms are found to be operative.

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