Jump to main content
Jump to site search

Issue 0, 1984
Previous Article Next Article

Specific enzyme inhibitors in vitamin biosynthesis. Part 6. Identification of an affinity chromatography ligand for the purification of riboflavin synthase

Abstract

The carbodi-imide-mediated condensation of the 7-oxolumazine (1) with amino-functionalised Sepharose at pH 4–5 gave a polymeric material which was effective in the purification of riboflavin synthase by affinity chromatography. The u.v. chromophore of this polymer-supported material was different from that of the 7-oxolumazine. Investigation of an analogous model reaction in free solution has led to a tentative identification of this affinity ligand. An explanation for the ability of this compound to bind to the enzyme is presented which suggests that it may be a ‘reaction co-ordinate’ analogue.

Back to tab navigation
Please wait while Download options loads

Article type: Paper
DOI: 10.1039/P19840000959
Citation: J. Chem. Soc., Perkin Trans. 1, 1984, 959-963
  •   Request permissions

    Specific enzyme inhibitors in vitamin biosynthesis. Part 6. Identification of an affinity chromatography ligand for the purification of riboflavin synthase

    R. Wrigglesworth, W. D. Inglis, D. B. Livingstone, C. J. Suckling and H. C. S. Wood, J. Chem. Soc., Perkin Trans. 1, 1984, 959
    DOI: 10.1039/P19840000959

Search articles by author