Abstract
Fluorescence quenching of benzo[ a]pyrene (BP) by cytochrome P-450 1A1 was used to probe the effect of the lipid, dilauroyl- l-3-phophatidylcholine, on this substrate-enzyme interaction. In the presence of lipid, a monoclonal antibody to this P-450 maximally inhibited BP binding at an antibody-to- P-450 ratio of 1:2, corresponding to an antibody crosslinked P-450 complex. The antibody did not inhibit BP binding in the absence of lipid. These results indicate that when P-450 is subjected to the orientational constraints imposed by antibody-mediated crosslinking, the lipid alters the conformation or quanternary structure of the P-450 oligomer in a manner which changes its affinity for BP.
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