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Updated: Sep 10, 2026
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Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
Purification of the flavin-containing monooxygenase from mouse and pig liver microsomes
The International Journal of Biochemistry
|January 1, 1984
Abstract:
The microsomal flavin-containing monooxygenase has been purified from mouse and pig liver utilizing Cibacron-Blue Sepharose, Procion-Red agarose, and 2'5'-ADP Sepharose. The enzymes had a final specific activity of 1200 and 954 nmol/min/mg protein from mouse and pig liver respectively. The enzyme from both mouse and pig liver displayed typical flavoprotein spectra and appeared homogeneous by denaturing polyacrylamide gel electrophoresis.
