Abstract
Using temperature as a perturbant, we have shown that mixed function amine oxidase undergoes structural changes in vitro which are correlated with changes in oxidative activity toward methimazole and N,N-diethylaniline. The observed changes between 30°-40° are irreversible, as shown by fluorescence, circular dichroism, and kinetic measurements. Although these studies show that the enzyme is remarkably sensitive to heat, in vivo properties may be different owing to possible endogenous ligands and lipid environment. The techniques used are sensitive and have potential for selective monitoring of mixed function amine oxidase properties in biological systems.
ACKNOWLEDGMENTS We thank Dr. Dan Ziegler, University of Texas, for his most generous gift of purified mixed function amine oxidase. We are grateful to Dr. Robert Henkens, Department of Chemistry, Duke University, for the use of his Perkin-Elmer MPF-3 spectrofluorimeter.
- Copyright © 1978 by Academic Press, Inc.
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