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Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
Inexpensive purification of P450 reductase and other proteins using 2',5'-adenosine diphosphate agarose affinity
1Department of Chemistry, Washington State University, Pullman, WA 99164-4630, USA. DAR73@mailcity.com
Protein Expression and Purification
|June 5, 2001
Abstract:
Two reductases, P450 oxidoreductase and P450Bm-3 reductase, were purified on a 2',5'-adenosine diphosphate solid support. Although the efficiency of these columns is well established, the cost of the resin and the eluting material 2'-adenosine can be prohibitive. Herein we show that the less costly 2',3'-adenosine monophosphate is an excellent eluting material.
