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.
MolPharm articles become freely available 12 months after publication, and remain freely available for 5 years.Non-open access articles that fall outside this five year window are available only to institutional subscribers and current ASPET members, or through the article purchase feature at the bottom of the page.
|
Log in using your username and password
Purchase access
In this issue
The Effect of Temperature on Mixed Function Amine Oxidase Intrinsic Fluorescence and Oxidative Activity
