Effects of Ni2+, Co2+, and Mn2+ on Desensitized Butyrylcholinesterase Prepared from Human Serum
Human serum butyrylcholinesterase (BChE) has been converted into a stable but less active desensitized form when heated at 45°C for 24 h. The desensitized BChE follows Michaelis-Menten kinetics, whereas native enzyme exhibits slightly negative cooperativity with respect to butyrylthiocholine binding...
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Veröffentlicht in: | Biological trace element research 2003-06, Vol.93 (1-3), p.55-62 |
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description | Human serum butyrylcholinesterase (BChE) has been converted into a stable but less active desensitized form when heated at 45°C for 24 h. The desensitized BChE follows Michaelis-Menten kinetics, whereas native enzyme exhibits slightly negative cooperativity with respect to butyrylthiocholine binding. In this study, we investigated the effects of Ni^sup 2+^, Co^sup 2+^, and Mn^sup 2+^ on the desensitized BChE. It is found that all three ions were noncompetitive inhibitors of the desensitized BChE, and K ^sub i^ values have been determined as 7.816±1.060 mM, 48.722±4.635 mM, and 84.795±5.249 mM for Ni^sup 2+^, Co^sup 2+^, and Mn^sup 2+^, respectively. In our previous study, these ions were linear mixed-type inhibitors of the native BChE. This finding confirms that desensitized BChE changes to a different conformation than native BChE. From the comparison of K ^sub i^ values of the trace elements, it can be said that Ni^sup 2+^ is a more effective inhibitor of the desensitized BChE than Co^sup 2+^ and Mn^sup 2+^.[PUBLICATION ABSTRACT] |
doi_str_mv | 10.1385/BTER:93:1-3:55 |
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Nese ; Tezcan, E. Ferhan</creator><creatorcontrib>Cengiz, Dogan ; Cokugras, A. Nese ; Tezcan, E. Ferhan</creatorcontrib><description>Human serum butyrylcholinesterase (BChE) has been converted into a stable but less active desensitized form when heated at 45°C for 24 h. The desensitized BChE follows Michaelis-Menten kinetics, whereas native enzyme exhibits slightly negative cooperativity with respect to butyrylthiocholine binding. In this study, we investigated the effects of Ni^sup 2+^, Co^sup 2+^, and Mn^sup 2+^ on the desensitized BChE. It is found that all three ions were noncompetitive inhibitors of the desensitized BChE, and K ^sub i^ values have been determined as 7.816±1.060 mM, 48.722±4.635 mM, and 84.795±5.249 mM for Ni^sup 2+^, Co^sup 2+^, and Mn^sup 2+^, respectively. In our previous study, these ions were linear mixed-type inhibitors of the native BChE. This finding confirms that desensitized BChE changes to a different conformation than native BChE. From the comparison of K ^sub i^ values of the trace elements, it can be said that Ni^sup 2+^ is a more effective inhibitor of the desensitized BChE than Co^sup 2+^ and Mn^sup 2+^.[PUBLICATION ABSTRACT]</description><identifier>ISSN: 0163-4984</identifier><identifier>EISSN: 0163-4984</identifier><identifier>EISSN: 1559-0720</identifier><identifier>DOI: 10.1385/BTER:93:1-3:55</identifier><language>eng</language><publisher>Clifton: Springer Nature B.V</publisher><subject>Cobalt ; Enzymes ; Ions ; Trace elements</subject><ispartof>Biological trace element research, 2003-06, Vol.93 (1-3), p.55-62</ispartof><rights>Humana Press Inc. 2003</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids></links><search><creatorcontrib>Cengiz, Dogan</creatorcontrib><creatorcontrib>Cokugras, A. 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This finding confirms that desensitized BChE changes to a different conformation than native BChE. 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Nese</au><au>Tezcan, E. Ferhan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effects of Ni2+, Co2+, and Mn2+ on Desensitized Butyrylcholinesterase Prepared from Human Serum</atitle><jtitle>Biological trace element research</jtitle><date>2003-06-01</date><risdate>2003</risdate><volume>93</volume><issue>1-3</issue><spage>55</spage><epage>62</epage><pages>55-62</pages><issn>0163-4984</issn><eissn>0163-4984</eissn><eissn>1559-0720</eissn><abstract>Human serum butyrylcholinesterase (BChE) has been converted into a stable but less active desensitized form when heated at 45°C for 24 h. The desensitized BChE follows Michaelis-Menten kinetics, whereas native enzyme exhibits slightly negative cooperativity with respect to butyrylthiocholine binding. In this study, we investigated the effects of Ni^sup 2+^, Co^sup 2+^, and Mn^sup 2+^ on the desensitized BChE. It is found that all three ions were noncompetitive inhibitors of the desensitized BChE, and K ^sub i^ values have been determined as 7.816±1.060 mM, 48.722±4.635 mM, and 84.795±5.249 mM for Ni^sup 2+^, Co^sup 2+^, and Mn^sup 2+^, respectively. In our previous study, these ions were linear mixed-type inhibitors of the native BChE. This finding confirms that desensitized BChE changes to a different conformation than native BChE. From the comparison of K ^sub i^ values of the trace elements, it can be said that Ni^sup 2+^ is a more effective inhibitor of the desensitized BChE than Co^sup 2+^ and Mn^sup 2+^.[PUBLICATION ABSTRACT]</abstract><cop>Clifton</cop><pub>Springer Nature B.V</pub><doi>10.1385/BTER:93:1-3:55</doi><tpages>8</tpages></addata></record> |
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title | Effects of Ni2+, Co2+, and Mn2+ on Desensitized Butyrylcholinesterase Prepared from Human Serum |
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