Methods used to resolve reversible flavoproteins into the constituents apoflavoprotein and prosthetic group

F. Müller, W.J.H. van Berkel

Research output: Chapter in Book/Report/Conference proceedingChapterAcademicpeer-review

Abstract

There are two classes of flavoproteins with respect to the interaction between the apoflavoprotein and its prosthetic group. In one class, the flavin is often tightly, but noncovalently bound. In the other class, the interaction between the two components is of covalent nature, the flavin being attached to an amino acid residue. This chapter discusses the most commonly used procedures for the preparation of apoflavoproteins. Although the development of methods for the reversible resolution of flavoproteins can be tedious and time consuming, especially when the goal is the achievement of a high reconstitutability, some studies should be included in the basic work done to characterize a new flavoprotein. Although the covalent chromatography method could be applied to any flavoprotein possessing an easily accessible sulfhydryl group, the method probably does not always give satisfactory results. The acid ammonium sulfate treatment is a rapid method to probe the possible preparation and stability/reconstitutability of apoflavoproteins on an analytical scale.
Original languageEnglish
Title of host publicationChemistry and biochemistry of flavoenzymes, F. Müller (ed.). Vol. 1. CRC Press, Boca Raton
EditorsFranz Muller
PublisherCRC Press
Chapter9
Pages261-274
Volume1
ISBN (Electronic)9781351079020
DOIs
Publication statusPublished - 1991

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