SCHEDULED MAINTENANCE
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.
C. J. Suckling, J. R. Sweeney and H. C. S. Wood, J. Chem. Soc., Perkin Trans. 1, 1977, 439 DOI: 10.1039/P19770000439
To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.
If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.
If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.
Read more about how to correctly acknowledge RSC content.
Please wait while we load your content...