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Volumn 119-120, Issue , 1999, Pages 165-171

Catalytic parameters for the hydrolysis of butyrylthiocholine by human serum butyrylcholinesterase variants

Author keywords

Butyrylcholinesterase; Catalytic constants; Human serum cholinesterase phenotypes genotypes; Substrate activation inhibition; Substrate binding sites

Indexed keywords

BUTYRYLTHIOCHOLINE; CHOLINESTERASE; ENZYME VARIANT;

EID: 0345085497     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(99)00025-3     Document Type: Conference Paper
Times cited : (4)

References (19)
  • 2
    • 0026031111 scopus 로고
    • Role of the peripheral anionic site on acetylcholinesterase: Inhibition by substrates and coumarin derivatives
    • Radić Z., Reiner E., Taylor P. Role of the peripheral anionic site on acetylcholinesterase: inhibition by substrates and coumarin derivatives. Mol. Pharmacol. 39:1991;98-104.
    • (1991) Mol. Pharmacol. , vol.39 , pp. 98-104
    • Radić, Z.1    Reiner, E.2    Taylor, P.3
  • 4
    • 0023605724 scopus 로고
    • Horse serum butyrylcholinesterase kinetics: A molecular mechanism based on inhibition studies with dansylaminoethyltrimethylammonium
    • Cauet G., Friboulet A., Thomas D. Horse serum butyrylcholinesterase kinetics: a molecular mechanism based on inhibition studies with dansylaminoethyltrimethylammonium. Biochem. Cell. Biol. 65:1987;529-535.
    • (1987) Biochem. Cell. Biol. , vol.65 , pp. 529-535
    • Cauet, G.1    Friboulet, A.2    Thomas, D.3
  • 5
    • 0027273738 scopus 로고
    • Recombinant human butyrylcholinesterase G390V, the fluoride-2 variant, expressed in Chinese hamster ovary cells, is a low affinity variant
    • Masson P., Adkins S., Gouet P., Lockridge O. Recombinant human butyrylcholinesterase G390V, the fluoride-2 variant, expressed in Chinese hamster ovary cells, is a low affinity variant. J. Biol. Chem. 268:1993;14329-14341.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14329-14341
    • Masson, P.1    Adkins, S.2    Gouet, P.3    Lockridge, O.4
  • 6
    • 0029665127 scopus 로고    scopus 로고
    • Asp.70 in the peripheral anionic site of human butyrylcholinesterase
    • Masson P., Froment M.T., Bartels C.F., Lockridge O. Asp.70 in the peripheral anionic site of human butyrylcholinesterase. Eur. J. Biochem. 235:1996;36-48.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 36-48
    • Masson, P.1    Froment, M.T.2    Bartels, C.F.3    Lockridge, O.4
  • 7
    • 0031043533 scopus 로고    scopus 로고
    • Role of aspartate 70 and tryptophane 82 in binding of succinyldithiocholine to human butyrylcholinesterase
    • Masson P., Legrand P., Bartels C.F., Froment M.-T., Schopfer L.M., Lockridge O. Role of aspartate 70 and tryptophane 82 in binding of succinyldithiocholine to human butyrylcholinesterase. Biochemistry. 36:1997;2266-2277.
    • (1997) Biochemistry , vol.36 , pp. 2266-2277
    • Masson, P.1    Legrand, P.2    Bartels, C.F.3    Froment, M.-T.4    Schopfer, L.M.5    Lockridge, O.6
  • 8
    • 0029847351 scopus 로고    scopus 로고
    • Binding sites on acetylcholinesterase and butyrylcholinesterase for pyridinium and imidazolium oximes, and other reversible ligands
    • Reiner E., Škrinjarić-Špoljar M., Simeon-Rudolf V. Binding sites on acetylcholinesterase and butyrylcholinesterase for pyridinium and imidazolium oximes, and other reversible ligands. Period. biol. 98:1996;325-329.
    • (1996) Period. Biol. , vol.98 , pp. 325-329
    • Reiner, E.1    Škrinjarić-Špoljar, M.2    Simeon-Rudolf, V.3
  • 9
    • 0016157081 scopus 로고
    • A steady-state kinetic model of butyrylcholinesterase from horse plasma
    • Augustinsson K.-B., Bartfai T., Mannervik B. A steady-state kinetic model of butyrylcholinesterase from horse plasma. Biochem. J. 141:1974;825-834.
    • (1974) Biochem. J. , vol.141 , pp. 825-834
    • Augustinsson, K.-B.1    Bartfai, T.2    Mannervik, B.3
  • 10
    • 0027517144 scopus 로고
    • Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- And butyrylcholinesterase inhibitors
    • Radić Z., Pickering N.A., Vellom D.C., Camp S., Taylor P. Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors. Biochemistry. 32:1993;12074-12084.
    • (1993) Biochemistry , vol.32 , pp. 12074-12084
    • Radić, Z.1    Pickering, N.A.2    Vellom, D.C.3    Camp, S.4    Taylor, P.5
  • 11
    • 0022569390 scopus 로고
    • Cholinesterase phenotyping: Clinical aspects and laboratory applications
    • Evans R.T. Cholinesterase phenotyping: clinical aspects and laboratory applications. CRC Crit. Rev. Clin. Lab. Sci. 23:1986;35-64.
    • (1986) CRC Crit. Rev. Clin. Lab. Sci. , vol.23 , pp. 35-64
    • Evans, R.T.1
  • 12
    • 0002221497 scopus 로고
    • Cholinesterase
    • Beckman L. Basel: Karger
    • Whittaker M. Cholinesterase. Beckman L. Monographs in Human Genetics. 11:1986;1-132 Karger, Basel.
    • (1986) Monographs in Human Genetics , vol.11 , pp. 1-132
    • Whittaker, M.1
  • 14
    • 0025294717 scopus 로고
    • Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine
    • Lockridge O. Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine. Pharmacol. Ther. 47:1990;35-60.
    • (1990) Pharmacol. Ther. , vol.47 , pp. 35-60
    • Lockridge, O.1
  • 16
    • 0343028026 scopus 로고
    • Kinetic studies on the hydrolysis of benzoylcholine by human serum cholinesterase
    • Kalow W., Genest K., Staron N. Kinetic studies on the hydrolysis of benzoylcholine by human serum cholinesterase. Can. J. Biochem. Physiol. 34:1956;637-653.
    • (1956) Can. J. Biochem. Physiol. , vol.34 , pp. 637-653
    • Kalow, W.1    Genest, K.2    Staron, N.3
  • 17
    • 0000452762 scopus 로고
    • Cholinesterase phenotyping and distribution of activity in sera of 346 individuals
    • Simeon V., Buntić A., Šurina B., Flegar-Meštrić Z. Cholinesterase phenotyping and distribution of activity in sera of 346 individuals. Acta Pharm. 37:1987;107-114.
    • (1987) Acta Pharm. , vol.37 , pp. 107-114
    • Simeon, V.1    Buntić, A.2    Šurina, B.3    Flegar-Meštrić, Z.4
  • 18
    • 0026659642 scopus 로고
    • DNA mutations associated with the human butyrylcholinesterase J-variant
    • Bartels C.F., James K., La Du B.N. DNA mutations associated with the human butyrylcholinesterase J-variant. Am. J. Hum. Genet. 50:1992;1104-1114.
    • (1992) Am. J. Hum. Genet. , vol.50 , pp. 1104-1114
    • Bartels, C.F.1    James, K.2    La Du, B.N.3
  • 19
    • 0016823110 scopus 로고
    • Interaction of fluorescence probes with acetylcholinesterase: The site and specificity of propidium binding
    • Taylor P., Lappi S. Interaction of fluorescence probes with acetylcholinesterase: the site and specificity of propidium binding. Biochemistry. 14:1975;1989-1997.
    • (1975) Biochemistry , vol.14 , pp. 1989-1997
    • Taylor, P.1    Lappi, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.