THE SUBMITOCHONDRIAL LOCALIZATION OF MONOAMINE OXIDASE
نویسندگان
چکیده
منابع مشابه
The Submitochondrial Localization of Monoamine Oxidase
Controlled osmotic lysis (water-washing) of rat liver mitochondria results in a mixed population of small vesicles derived mainly from the outer mitochondrial membrane and of larger bodies containing a few cristae derived from the inner membrane. These elements have been separated on Ficoll and sucrose gradients. The small vesicles were rich in monoamine oxidase, and the large bodies were rich ...
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Monoamine oxidase B (MAO-B) was recently identified as a member of the family of imidazoline binding proteins. To localize the imidazoline binding domain on MAO-B, we labeled the domain with the imidazoline photoaffinity adduct [125I]2-(3-azido-4-iodophenoxy)methylimidazoline in rat and human liver and visualized labeled peptides by autoradiography/sodium dodecyl sulfate-polyacrylamide gel elec...
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Seven stilbenes and one catechin were bioactivity-guidedly isolated from the rhizomes of Rheum palmatem. Their structures were identified as piceatannol(1), resveratrol(2), piceid(3), rhapontigenin(4), piceatannol-3'-O-β-D-glucopyranoside(5), rhaponticin(6), catechin(7) and desoxyrhapontigenin(8). Anti-monoamine oxidase (MAO) activities of compounds 1–8 were tested. Compounds 1 and 8 showed sig...
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Monoamine oxidase (MAO) oxidatively deaminates vasoactive and biogenic amines and exists in two distinct forms (A and B), coded for by separate genes, which exhibit distinct substrate specificities and inhibitor sensitivities. Using specific primers for MAO-A and MAO-B mRNA in a reverse transcription-polymerase chain reaction (RT-PCR) on RNA from human liver, the predicted products for both enz...
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Numerous studies have been reported concerning the role of monoamine oxidase (MAO) in the metabolism of biogenic amines, especially in the central nervous system and in the heart. A large number of compounds that inhibit MAO have been described, and some of these have been used therapeutically. For this reason we considered that differences in concentration and localization of the enzyme might ...
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ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 1967
ISSN: 1540-8140,0021-9525
DOI: 10.1083/jcb.32.3.719