Dihydropteroate synthase: purification by affinity chromatography and mechanism of action
- 1 January 1977
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Journal of the Chemical Society, Perkin Transactions 1
- Vol. 4 (4) , 439-442
- https://doi.org/10.1039/p19770000439
Abstract
The purification of dihydropteroate synthase by affinity chromatography on a sulphonamide bound to agarose is described. The discovery that binding to the affinity column occurs only in the presence of the co-substrate, the pteridine diphosphate (2), or the corresponding monophosphate (3), is discussed in relation to an ordered kinetic mechanism of action of the enzyme.This publication has 4 references indexed in Scilit:
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