TAILIEUCHUNG - Báo cáo khoa học: Kinetic analysis of effector modulation of butyrylcholinesterase-catalysed hydrolysis of acetanilides and homologous esters

Tham khảo luận văn - đề án 'báo cáo khoa học: kinetic analysis of effector modulation of butyrylcholinesterase-catalysed hydrolysis of acetanilides and homologous esters', luận văn - báo cáo, báo cáo khoa học phục vụ nhu cầu học tập, nghiên cứu và làm việc hiệu quả | ỊFEBS Journal Kinetic analysis of effector modulation of butyrylcholinesterase-catalysed hydrolysis of acetanilides and homologous esters Patrick Masson1 Marie-Thérèse Froment1 Emilie Gillon1 Florian Nachon1 Oksana Lockridge2 and Lawrence M. Schopfer2 1 Unite d Enzymologie Departement de Toxicologie Centre de Recherches du Service de Sante des Armees La Tronche Cedex France 2 University of Nebraska MedicalCenter Eppley Institute Omaha NE USA Keywords aryl acylamidase benzalkonium butyrylcholinesterase serotonin tyramine Correspondence P. Masson Unite d Enzymologie Departement de Toxicologie Centre de Recherches du Service de Sante des Armees BP 87 38702 La Tronche Cedex France Fax 33 4 76 63 69 62 Tel 33 4 76 63 69 59 E-mail pmasson@ Received 30 December 2007 revised 27 February 2008 accepted 17 March 2008 doi The effects of tyramine serotonin and benzalkonium on the esterase and aryl acylamidase activities of wild-type human butyrylcholinesterase and its peripheral anionic site mutant D70G were investigated. The kinetic study was carried out under steady-state conditions with neutral and positively charged aryl acylamides o-nitrophenylacetanilide o-nitrotrifluoropheny-lacetanilide and m- acetamido N N N-trimethylanilinium and homologous esters o-nitrophenyl acetate and acetylthiocholine . Tyramine was an activator of hydrolysis for neutral substrates and an inhibitor of hydrolysis for positively charged substrates. The affinity of D70G for tyramine was lower than that of the wild-type enzyme. Tyramine activation of hydrolysis for neutral substrates by D70G was linear. Tyramine was found to be a pure competitive inhibitor of hydrolysis for positively charged substrates with both wild-type butyrylcholinesterase and D70G. Serotonin inhibited both esterase and aryl acylamidase activities for both positively charged and neutral substrates. Inhibition of wild-type butyrylcholinesterase was hyperbolic . partial with neutral .

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