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Purification of rat liver monoamine oxidase by octyl glucoside extraction and reconstitution
Authors:Mark A. Stadt  Peter A. Banks  Rodger D. Kobes
Affiliation:Department of Biochemistry, Michigan State University, East Lansing, Michigan 48824 USA
Abstract:
Catalytically active isoenzymes of rat liver monoamine oxidase have been copurified from the outer mitochondrial membrane by a novel method involving repetitive solubilization with octyl-β-d-glucopyranoside followed by reconstitution into lipid vesicles. As analyzed using sodium dodecyl sulfate-gel electrophoresis, the purified enzyme migrates as a single band of protein of molecular weight 60,000. The preparation is capable of metabolizing 576 nmol serotonin and 777 nmol β-phenylethylamine/min/mg protein. Apparent Km values and sensitivity to the inhibitor clorgyline are very similar for the purified and outer mitochondrial membrane-bound enzyme when determined with the substrates β-phenylethylamine, serotonin, and tyramine.
Keywords:To whom correspondence should be addressed.
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