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- W958641337 abstract "This chapter discusses the methods of preparation of monoamine oxidase (Human serum or plasma). The enzyme oxidizes primary amines without α-substituents. Although it deaminates ethanolamine, it does not oxidize β-substituted ethanolamines. Its best substrates are relatively apolar amines and include C-arylmethylamines as well as simple aliphatic amines. Less actively oxidized substrates include kynuramine, tryptamine, and tyramine. Unlike the rabbit serum enzyme, the human enzyme is competitively inhibited by aliphatic alcohols and its activity decreases in the presence of high concentrations of substrates without polar substituents. The substrate inhibition fits the Haldane equation, is more apparent with long-chain n-alkylamines than with their short-chain homologs, and is most apparent at pH values that provide significant concentrations of unprotonated species of amines. These and other findings suggest that the enzyme's active center has both electrophilic and hydrophobic binding sites. Elevated levels of the serum enzyme have been found in adults with Laennec's and post-necrotic cirrhosis, massive neoplastic replacement of the liver, hepatic sarcoidosis, and chronic congestive heart failure." @default.
- W958641337 created "2016-06-24" @default.
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- W958641337 date "1971-01-01" @default.
- W958641337 modified "2023-09-26" @default.
- W958641337 title "[231] Monoamine oxidase (human serum or plasma)" @default.
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- W958641337 doi "https://doi.org/10.1016/0076-6879(71)17120-0" @default.
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