Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method

Abstract The in vitro effect of technical grade malathion was assessed via the kinetic parameters of human plasma butyrylcholinesterase (BChE) using N-methylindoxyl acetate as a substrate for BChE. An inhibitor kinetics study demonstrated the existence of a biphasic inhibition curve, indicating high...
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Autor*in:	Pavelkić, V. M. [verfasserIn] Krinulović, K. S. Savić, J. Z. Ilić, M. A.

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2008

Schlagwörter:	Cholinesterase Malathion Inhibition Curve BChE Activity Malaoxon

Anmerkung:	© MAIK Nauka 2008

Übergeordnetes Werk:	Enthalten in: Russian journal of physical chemistry - Berlin : Springer Science+Business Media, 2007, 82(2008), 5 vom: Mai, Seite 870-874
Übergeordnetes Werk:	volume:82 ; year:2008 ; number:5 ; month:05 ; pages:870-874

Links:	Volltext

DOI / URN:	10.1134/S0036024408050312

Katalog-ID:	SPR020329415

Internformat


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100	1		\|a Pavelkić, V. M. \|e verfasserin \|4 aut
245	1	0	\|a Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method
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520			\|a Abstract The in vitro effect of technical grade malathion was assessed via the kinetic parameters of human plasma butyrylcholinesterase (BChE) using N-methylindoxyl acetate as a substrate for BChE. An inhibitor kinetics study demonstrated the existence of a biphasic inhibition curve, indicating high-and low-affinity binding sites of malathion. The IC50 values as calculated from the experimental inhibition curves were 1.33 × $ 10^{−9} $ and 1.48 × $ 10^{−5} $ M for the high-and low-affinity binding sites, respectively; Hill’s analysis gave 1.29 × $ 10^{−9} $ and 1.38 × $ 10^{−6} $ M. The Cornish-Bowden plots and their secondary plots indicated that the nature of inhibition was of mixed type with the predominant competitive character of both affinity binding sites.
650		4	\|a Cholinesterase \|7 (dpeaa)DE-He213
650		4	\|a Malathion \|7 (dpeaa)DE-He213
650		4	\|a Inhibition Curve \|7 (dpeaa)DE-He213
650		4	\|a BChE Activity \|7 (dpeaa)DE-He213
650		4	\|a Malaoxon \|7 (dpeaa)DE-He213
700	1		\|a Krinulović, K. S. \|4 aut
700	1		\|a Savić, J. Z. \|4 aut
700	1		\|a Ilić, M. A. \|4 aut
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912			\|a GBV_ILN_150
912			\|a GBV_ILN_151
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912			\|a GBV_ILN_170
912			\|a GBV_ILN_171
912			\|a GBV_ILN_187
912			\|a GBV_ILN_213
912			\|a GBV_ILN_224
912			\|a GBV_ILN_230
912			\|a GBV_ILN_250
912			\|a GBV_ILN_281
912			\|a GBV_ILN_285
912			\|a GBV_ILN_293
912			\|a GBV_ILN_370
912			\|a GBV_ILN_602
912			\|a GBV_ILN_636
912			\|a GBV_ILN_702
912			\|a GBV_ILN_2001
912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2004
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912			\|a GBV_ILN_2006
912			\|a GBV_ILN_2007
912			\|a GBV_ILN_2008
912			\|a GBV_ILN_2009
912			\|a GBV_ILN_2010
912			\|a GBV_ILN_2011
912			\|a GBV_ILN_2014
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2021
912			\|a GBV_ILN_2025
912			\|a GBV_ILN_2026
912			\|a GBV_ILN_2027
912			\|a GBV_ILN_2031
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912			\|a GBV_ILN_2038
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912			\|a GBV_ILN_2044
912			\|a GBV_ILN_2048
912			\|a GBV_ILN_2049
912			\|a GBV_ILN_2050
912			\|a GBV_ILN_2055
912			\|a GBV_ILN_2057
912			\|a GBV_ILN_2059
912			\|a GBV_ILN_2061
912			\|a GBV_ILN_2064
912			\|a GBV_ILN_2065
912			\|a GBV_ILN_2068
912			\|a GBV_ILN_2070
912			\|a GBV_ILN_2086
912			\|a GBV_ILN_2088
912			\|a GBV_ILN_2093
912			\|a GBV_ILN_2106
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912			\|a GBV_ILN_2108
912			\|a GBV_ILN_2110
912			\|a GBV_ILN_2111
912			\|a GBV_ILN_2112
912			\|a GBV_ILN_2113
912			\|a GBV_ILN_2116
912			\|a GBV_ILN_2118
912			\|a GBV_ILN_2119
912			\|a GBV_ILN_2122
912			\|a GBV_ILN_2129
912			\|a GBV_ILN_2143
912			\|a GBV_ILN_2144
912			\|a GBV_ILN_2147
912			\|a GBV_ILN_2148
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912			\|a GBV_ILN_2190
912			\|a GBV_ILN_2232
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912			\|a GBV_ILN_2446
912			\|a GBV_ILN_2470
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912			\|a GBV_ILN_4012
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912			\|a GBV_ILN_4037
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912			\|a GBV_ILN_4325
912			\|a GBV_ILN_4326
912			\|a GBV_ILN_4333
912			\|a GBV_ILN_4334
912			\|a GBV_ILN_4335
912			\|a GBV_ILN_4336
912			\|a GBV_ILN_4338
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Indexfelder

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publishDate	2008
allfields	10.1134/S0036024408050312 doi (DE-627)SPR020329415 (SPR)S0036024408050312-e DE-627 ger DE-627 rakwb eng Pavelkić, V. M. verfasserin aut Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © MAIK Nauka 2008 Abstract The in vitro effect of technical grade malathion was assessed via the kinetic parameters of human plasma butyrylcholinesterase (BChE) using N-methylindoxyl acetate as a substrate for BChE. An inhibitor kinetics study demonstrated the existence of a biphasic inhibition curve, indicating high-and low-affinity binding sites of malathion. The IC50 values as calculated from the experimental inhibition curves were 1.33 × $ 10^{−9} $ and 1.48 × $ 10^{−5} $ M for the high-and low-affinity binding sites, respectively; Hill’s analysis gave 1.29 × $ 10^{−9} $ and 1.38 × $ 10^{−6} $ M. The Cornish-Bowden plots and their secondary plots indicated that the nature of inhibition was of mixed type with the predominant competitive character of both affinity binding sites. Cholinesterase (dpeaa)DE-He213 Malathion (dpeaa)DE-He213 Inhibition Curve (dpeaa)DE-He213 BChE Activity (dpeaa)DE-He213 Malaoxon (dpeaa)DE-He213 Krinulović, K. S. aut Savić, J. Z. aut Ilić, M. A. aut Enthalten in Russian journal of physical chemistry Berlin : Springer Science+Business Media, 2007 82(2008), 5 vom: Mai, Seite 870-874 (DE-627)633755036 (DE-600)2569139-9 1531-863X nnns volume:82 year:2008 number:5 month:05 pages:870-874 https://dx.doi.org/10.1134/S0036024408050312 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 82 2008 5 05 870-874
spelling	10.1134/S0036024408050312 doi (DE-627)SPR020329415 (SPR)S0036024408050312-e DE-627 ger DE-627 rakwb eng Pavelkić, V. M. verfasserin aut Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © MAIK Nauka 2008 Abstract The in vitro effect of technical grade malathion was assessed via the kinetic parameters of human plasma butyrylcholinesterase (BChE) using N-methylindoxyl acetate as a substrate for BChE. An inhibitor kinetics study demonstrated the existence of a biphasic inhibition curve, indicating high-and low-affinity binding sites of malathion. The IC50 values as calculated from the experimental inhibition curves were 1.33 × $ 10^{−9} $ and 1.48 × $ 10^{−5} $ M for the high-and low-affinity binding sites, respectively; Hill’s analysis gave 1.29 × $ 10^{−9} $ and 1.38 × $ 10^{−6} $ M. The Cornish-Bowden plots and their secondary plots indicated that the nature of inhibition was of mixed type with the predominant competitive character of both affinity binding sites. Cholinesterase (dpeaa)DE-He213 Malathion (dpeaa)DE-He213 Inhibition Curve (dpeaa)DE-He213 BChE Activity (dpeaa)DE-He213 Malaoxon (dpeaa)DE-He213 Krinulović, K. S. aut Savić, J. Z. aut Ilić, M. A. aut Enthalten in Russian journal of physical chemistry Berlin : Springer Science+Business Media, 2007 82(2008), 5 vom: Mai, Seite 870-874 (DE-627)633755036 (DE-600)2569139-9 1531-863X nnns volume:82 year:2008 number:5 month:05 pages:870-874 https://dx.doi.org/10.1134/S0036024408050312 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 82 2008 5 05 870-874
allfields_unstemmed	10.1134/S0036024408050312 doi (DE-627)SPR020329415 (SPR)S0036024408050312-e DE-627 ger DE-627 rakwb eng Pavelkić, V. M. verfasserin aut Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © MAIK Nauka 2008 Abstract The in vitro effect of technical grade malathion was assessed via the kinetic parameters of human plasma butyrylcholinesterase (BChE) using N-methylindoxyl acetate as a substrate for BChE. An inhibitor kinetics study demonstrated the existence of a biphasic inhibition curve, indicating high-and low-affinity binding sites of malathion. The IC50 values as calculated from the experimental inhibition curves were 1.33 × $ 10^{−9} $ and 1.48 × $ 10^{−5} $ M for the high-and low-affinity binding sites, respectively; Hill’s analysis gave 1.29 × $ 10^{−9} $ and 1.38 × $ 10^{−6} $ M. The Cornish-Bowden plots and their secondary plots indicated that the nature of inhibition was of mixed type with the predominant competitive character of both affinity binding sites. Cholinesterase (dpeaa)DE-He213 Malathion (dpeaa)DE-He213 Inhibition Curve (dpeaa)DE-He213 BChE Activity (dpeaa)DE-He213 Malaoxon (dpeaa)DE-He213 Krinulović, K. S. aut Savić, J. Z. aut Ilić, M. A. aut Enthalten in Russian journal of physical chemistry Berlin : Springer Science+Business Media, 2007 82(2008), 5 vom: Mai, Seite 870-874 (DE-627)633755036 (DE-600)2569139-9 1531-863X nnns volume:82 year:2008 number:5 month:05 pages:870-874 https://dx.doi.org/10.1134/S0036024408050312 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 82 2008 5 05 870-874
allfieldsGer	10.1134/S0036024408050312 doi (DE-627)SPR020329415 (SPR)S0036024408050312-e DE-627 ger DE-627 rakwb eng Pavelkić, V. M. verfasserin aut Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © MAIK Nauka 2008 Abstract The in vitro effect of technical grade malathion was assessed via the kinetic parameters of human plasma butyrylcholinesterase (BChE) using N-methylindoxyl acetate as a substrate for BChE. An inhibitor kinetics study demonstrated the existence of a biphasic inhibition curve, indicating high-and low-affinity binding sites of malathion. The IC50 values as calculated from the experimental inhibition curves were 1.33 × $ 10^{−9} $ and 1.48 × $ 10^{−5} $ M for the high-and low-affinity binding sites, respectively; Hill’s analysis gave 1.29 × $ 10^{−9} $ and 1.38 × $ 10^{−6} $ M. The Cornish-Bowden plots and their secondary plots indicated that the nature of inhibition was of mixed type with the predominant competitive character of both affinity binding sites. Cholinesterase (dpeaa)DE-He213 Malathion (dpeaa)DE-He213 Inhibition Curve (dpeaa)DE-He213 BChE Activity (dpeaa)DE-He213 Malaoxon (dpeaa)DE-He213 Krinulović, K. S. aut Savić, J. Z. aut Ilić, M. A. aut Enthalten in Russian journal of physical chemistry Berlin : Springer Science+Business Media, 2007 82(2008), 5 vom: Mai, Seite 870-874 (DE-627)633755036 (DE-600)2569139-9 1531-863X nnns volume:82 year:2008 number:5 month:05 pages:870-874 https://dx.doi.org/10.1134/S0036024408050312 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 82 2008 5 05 870-874
allfieldsSound	10.1134/S0036024408050312 doi (DE-627)SPR020329415 (SPR)S0036024408050312-e DE-627 ger DE-627 rakwb eng Pavelkić, V. M. verfasserin aut Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method 2008 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © MAIK Nauka 2008 Abstract The in vitro effect of technical grade malathion was assessed via the kinetic parameters of human plasma butyrylcholinesterase (BChE) using N-methylindoxyl acetate as a substrate for BChE. An inhibitor kinetics study demonstrated the existence of a biphasic inhibition curve, indicating high-and low-affinity binding sites of malathion. The IC50 values as calculated from the experimental inhibition curves were 1.33 × $ 10^{−9} $ and 1.48 × $ 10^{−5} $ M for the high-and low-affinity binding sites, respectively; Hill’s analysis gave 1.29 × $ 10^{−9} $ and 1.38 × $ 10^{−6} $ M. The Cornish-Bowden plots and their secondary plots indicated that the nature of inhibition was of mixed type with the predominant competitive character of both affinity binding sites. Cholinesterase (dpeaa)DE-He213 Malathion (dpeaa)DE-He213 Inhibition Curve (dpeaa)DE-He213 BChE Activity (dpeaa)DE-He213 Malaoxon (dpeaa)DE-He213 Krinulović, K. S. aut Savić, J. Z. aut Ilić, M. A. aut Enthalten in Russian journal of physical chemistry Berlin : Springer Science+Business Media, 2007 82(2008), 5 vom: Mai, Seite 870-874 (DE-627)633755036 (DE-600)2569139-9 1531-863X nnns volume:82 year:2008 number:5 month:05 pages:870-874 https://dx.doi.org/10.1134/S0036024408050312 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 82 2008 5 05 870-874
language	English
source	Enthalten in Russian journal of physical chemistry 82(2008), 5 vom: Mai, Seite 870-874 volume:82 year:2008 number:5 month:05 pages:870-874
sourceStr	Enthalten in Russian journal of physical chemistry 82(2008), 5 vom: Mai, Seite 870-874 volume:82 year:2008 number:5 month:05 pages:870-874
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Cholinesterase Malathion Inhibition Curve BChE Activity Malaoxon
isfreeaccess_bool	false
container_title	Russian journal of physical chemistry
authorswithroles_txt_mv	Pavelkić, V. M. @@aut@@ Krinulović, K. S. @@aut@@ Savić, J. Z. @@aut@@ Ilić, M. A. @@aut@@
publishDateDaySort_date	2008-05-01T00:00:00Z
hierarchy_top_id	633755036
id	SPR020329415
language_de	englisch
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An inhibitor kinetics study demonstrated the existence of a biphasic inhibition curve, indicating high-and low-affinity binding sites of malathion. The IC50 values as calculated from the experimental inhibition curves were 1.33 × $ 10^{−9} $ and 1.48 × $ 10^{−5} $ M for the high-and low-affinity binding sites, respectively; Hill’s analysis gave 1.29 × $ 10^{−9} $ and 1.38 × $ 10^{−6} $ M. 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author	Pavelkić, V. M.
spellingShingle	Pavelkić, V. M. misc Cholinesterase misc Malathion misc Inhibition Curve misc BChE Activity misc Malaoxon Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method
authorStr	Pavelkić, V. M.
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topic_title	Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method Cholinesterase (dpeaa)DE-He213 Malathion (dpeaa)DE-He213 Inhibition Curve (dpeaa)DE-He213 BChE Activity (dpeaa)DE-He213 Malaoxon (dpeaa)DE-He213
topic	misc Cholinesterase misc Malathion misc Inhibition Curve misc BChE Activity misc Malaoxon
topic_unstemmed	misc Cholinesterase misc Malathion misc Inhibition Curve misc BChE Activity misc Malaoxon
topic_browse	misc Cholinesterase misc Malathion misc Inhibition Curve misc BChE Activity misc Malaoxon
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title	Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method
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title_full	Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method
author_sort	Pavelkić, V. M.
journal	Russian journal of physical chemistry
journalStr	Russian journal of physical chemistry
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author_browse	Pavelkić, V. M. Krinulović, K. S. Savić, J. Z. Ilić, M. A.
container_volume	82
format_se	Elektronische Aufsätze
author-letter	Pavelkić, V. M.
doi_str_mv	10.1134/S0036024408050312
title_sort	malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method
title_auth	Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method
abstract	Abstract The in vitro effect of technical grade malathion was assessed via the kinetic parameters of human plasma butyrylcholinesterase (BChE) using N-methylindoxyl acetate as a substrate for BChE. An inhibitor kinetics study demonstrated the existence of a biphasic inhibition curve, indicating high-and low-affinity binding sites of malathion. The IC50 values as calculated from the experimental inhibition curves were 1.33 × $ 10^{−9} $ and 1.48 × $ 10^{−5} $ M for the high-and low-affinity binding sites, respectively; Hill’s analysis gave 1.29 × $ 10^{−9} $ and 1.38 × $ 10^{−6} $ M. The Cornish-Bowden plots and their secondary plots indicated that the nature of inhibition was of mixed type with the predominant competitive character of both affinity binding sites. © MAIK Nauka 2008
abstractGer	Abstract The in vitro effect of technical grade malathion was assessed via the kinetic parameters of human plasma butyrylcholinesterase (BChE) using N-methylindoxyl acetate as a substrate for BChE. An inhibitor kinetics study demonstrated the existence of a biphasic inhibition curve, indicating high-and low-affinity binding sites of malathion. The IC50 values as calculated from the experimental inhibition curves were 1.33 × $ 10^{−9} $ and 1.48 × $ 10^{−5} $ M for the high-and low-affinity binding sites, respectively; Hill’s analysis gave 1.29 × $ 10^{−9} $ and 1.38 × $ 10^{−6} $ M. The Cornish-Bowden plots and their secondary plots indicated that the nature of inhibition was of mixed type with the predominant competitive character of both affinity binding sites. © MAIK Nauka 2008
abstract_unstemmed	Abstract The in vitro effect of technical grade malathion was assessed via the kinetic parameters of human plasma butyrylcholinesterase (BChE) using N-methylindoxyl acetate as a substrate for BChE. An inhibitor kinetics study demonstrated the existence of a biphasic inhibition curve, indicating high-and low-affinity binding sites of malathion. The IC50 values as calculated from the experimental inhibition curves were 1.33 × $ 10^{−9} $ and 1.48 × $ 10^{−5} $ M for the high-and low-affinity binding sites, respectively; Hill’s analysis gave 1.29 × $ 10^{−9} $ and 1.38 × $ 10^{−6} $ M. The Cornish-Bowden plots and their secondary plots indicated that the nature of inhibition was of mixed type with the predominant competitive character of both affinity binding sites. © MAIK Nauka 2008
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container_issue	5
title_short	Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method
url	https://dx.doi.org/10.1134/S0036024408050312
remote_bool	true
author2	Krinulović, K. S. Savić, J. Z. Ilić, M. A.
author2Str	Krinulović, K. S. Savić, J. Z. Ilić, M. A.
ppnlink	633755036
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doi_str	10.1134/S0036024408050312
up_date	2024-07-03T15:21:52.106Z
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Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method

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