Serotonin-sensitive aryl acylamidase activity of acetylcholinesterase
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Identification of serotonin-sensitive aryl acylamidase activity with cobra venom acetylcholinesterase.
Acetylcholinesterase purified from cobra (Naja naja) venom exhibits a serotonin-sensitive aryl acylamidase activity. Both acetylcholinesterase and aryl acylamidase activities co-eluted in column chromatographic procedures (Sephadex G-75 and Zinc-Sepharose), co-migrated on polyacrylamide gel electrophoresis, co-immunoprecipitated by anti-snake venom antibody and showed the same heat denaturation...
متن کاملThe association of the serotonin-sensitive aryl acylamidase with acetylcholinesterase in the monkey brain.
The serotonin-sensitive aryl acylamidase was partially purified from monkey brain. The aryl acylamidase activity was inhibited by serotonin (Ki = 0.425 mM) and tryptamine (Ki = 3.6 mM) but not by a number of other amines. It was also inhibited by acetylcholine (Ki = 2 mM) and its analogues and homologues. The relationship of aryl acylamidase to acetylcholinesterase was examined. The ratios of s...
متن کاملThe aryl acylamidases and their relationship to cholinesterases in human serum, erythrocyte and liver.
Human serum aryl acylamidase associated with serum cholinesterase was purified to homogeneity. Evidence for the identity of the two enzymes was based on co-elution profiles, co-purification in the different steps including affinity chromatography with constant ratios of specific activity and percentage recoveries, co-migration on gel electrophoresis, parallel inhibition by typical cholinesteras...
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-l. Significant levels of aryl acylamidase (E.C. 3.5.1:13) activity have been found in extracts of larvae of the webbing clothes moth, Tineola bisselliella using acetyl p-nitroanilide as substrate. 2. Gel electrophoresis suggests that the activity is due to more than one enzyme. Inhibitor studies show that these enzymes are probably of the "active serine" type but have a requirement for a free ...
متن کاملCharacterization of aryl acylamidase activity from propanil-resistant barnyardgrass (Echinochloa crus-galli [L.] Beauv.)
The enzyme, aryl acylamidase, was characterized in propanil-susceptible and propanil-resistant barnyardgrass with respect to kinetic parameters, the effects of inhibitors, and the levels of activity in darkand light-grown tissues. The enzyme reaction in the resistant tissue preparation proceeded linearly with time over a 5 h time course, while activity in the susceptible tissue preparation was ...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1976
ISSN: 0014-5793
DOI: 10.1016/0014-5793(76)80912-x