Abstract
where V, is the rate of product formation by the unactivated enzyme (E-S) and V/cl. by the activated enzyme (C-E-S), and K , is the true dissociation constant ( k z / k z ) describing the binding of apo-CII to substrate-bound LPL. Further steady-state experiments in which substrate and apo-CII concentrations were varied gave results which were predicted accurately by the above equation and, additionally, revealed that Vfc‘. is approximately 1.4 times greater than V, In conclusion, the study shows that apo-CII achieves activation in this system by associating preferentially with the form of the enzyme which is bound to the substrate ( K d = 7 1 2 n ~ ) rather than to the free species ( K d = 200nM). thus reducing the apparent K,. Activated LPL forms products at a rate which is only slightly greater than that of the unactivated enzyme.
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