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- W2012376814 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 K m 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." @default.
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- W2012376814 date "1982-03-01" @default.
- W2012376814 modified "2023-09-27" @default.
- W2012376814 title "Purification of rat liver monoamine oxidase by octyl glucoside extraction and reconstitution" @default.
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- W2012376814 doi "https://doi.org/10.1016/0003-9861(82)90025-x" @default.
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