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Pregled bibliografske jedinice broj: 93525

Comparison of two reaction schemes for the the hydrolysis of acetylthiocholine by butyrylcholinesterase


Simeon-Rudolf, Vera; Šinko, Goran; Štuglin, Anita; Stojan, Jure; Goličnik, Marko; Reiner, Elsa
Comparison of two reaction schemes for the the hydrolysis of acetylthiocholine by butyrylcholinesterase // XIth International Symposium on Cholinergic Mechanisms-Function and Disfunction & 2nd Mishrahi Symposium on Neurobiology, St. Moritz, Švicarska, Program and Abstracts
Sankt Moritz, 2002. str. 36-36 (poster, međunarodna recenzija, sažetak, znanstveni)


CROSBI ID: 93525 Za ispravke kontaktirajte CROSBI podršku putem web obrasca

Naslov
Comparison of two reaction schemes for the the hydrolysis of acetylthiocholine by butyrylcholinesterase

Autori
Simeon-Rudolf, Vera ; Šinko, Goran ; Štuglin, Anita ; Stojan, Jure ; Goličnik, Marko ; Reiner, Elsa

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
XIth International Symposium on Cholinergic Mechanisms-Function and Disfunction & 2nd Mishrahi Symposium on Neurobiology, St. Moritz, Švicarska, Program and Abstracts / - Sankt Moritz, 2002, 36-36

Skup
XIth International Symposium on Cholinergic Mechanisms-Function and Disfunction & 2nd Mishrahi Symposium on Neurobiology, St. Moritz

Mjesto i datum
St. Moritz, Švicarska, 05.05.2002. - 09.05.2002

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
butyrylcholinesterase; catalytic parameters; kinetic models

Sažetak
Catalytic parameters calculated from the schemes derived by Webb (Model A) and by Stojan (Model B) were compared for the hydrolysis of acetylthiocholine (ATCh) by purified horse serum butyrylcholinesterase (BChE) (measured by conventional and stopped-flow techniques). In Model A the acetylated enzyme is omitted from the scheme, while in Model B the Michaelis complex is omitted. The enzyme-substrate dissociation constants Ks and Kss in Model A were 0.25 and 2.0 mM (conv. tech.) and 0.17 and 6.3 mM (stopped-flow tech.). These were attributed to binding of ATCh to the catalytic and peripheral site of BChE. The constants K1 and K2 in Model B (stopped-flow tech.) were 0.223 and >1000 mM. These are attributed to binding of ATCh to an unidentified site in the free enzyme and to the peripheral site in the acetylated enzyme. As the Ks and K1 values are almost the same, both constants are likely to refer to the same enzyme-substrate complex. The constants Kss and K2 are very different ; they are both attributed to peripheral binding of ATCh, but they obviously refer to different complexes. Both models postulate that peripheral binding of a substrate affects rate constants of substrate hydrolysis ; this also follows from the evaluated constants for ATCh hydrolysis.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Kliničke medicinske znanosti



POVEZANOST RADA


Projekti:
00220104

Ustanove:
Institut za medicinska istraživanja i medicinu rada, Zagreb

Profili:

Avatar Url Vera Simeon (autor)

Avatar Url Goran Šinko (autor)

Avatar Url Anita Bosak (autor)

Avatar Url Elsa Reiner (autor)


Citiraj ovu publikaciju:

Simeon-Rudolf, Vera; Šinko, Goran; Štuglin, Anita; Stojan, Jure; Goličnik, Marko; Reiner, Elsa
Comparison of two reaction schemes for the the hydrolysis of acetylthiocholine by butyrylcholinesterase // XIth International Symposium on Cholinergic Mechanisms-Function and Disfunction & 2nd Mishrahi Symposium on Neurobiology, St. Moritz, Švicarska, Program and Abstracts
Sankt Moritz, 2002. str. 36-36 (poster, međunarodna recenzija, sažetak, znanstveni)
Simeon-Rudolf, V., Šinko, G., Štuglin, A., Stojan, J., Goličnik, M. & Reiner, E. (2002) Comparison of two reaction schemes for the the hydrolysis of acetylthiocholine by butyrylcholinesterase. U: XIth International Symposium on Cholinergic Mechanisms-Function and Disfunction & 2nd Mishrahi Symposium on Neurobiology, St. Moritz, Švicarska, Program and Abstracts.
@article{article, author = {Simeon-Rudolf, Vera and \v{S}inko, Goran and \v{S}tuglin, Anita and Stojan, Jure and Goli\v{c}nik, Marko and Reiner, Elsa}, year = {2002}, pages = {36-36}, keywords = {butyrylcholinesterase, catalytic parameters, kinetic models}, title = {Comparison of two reaction schemes for the the hydrolysis of acetylthiocholine by butyrylcholinesterase}, keyword = {butyrylcholinesterase, catalytic parameters, kinetic models}, publisherplace = {St. Moritz, \v{S}vicarska} }
@article{article, author = {Simeon-Rudolf, Vera and \v{S}inko, Goran and \v{S}tuglin, Anita and Stojan, Jure and Goli\v{c}nik, Marko and Reiner, Elsa}, year = {2002}, pages = {36-36}, keywords = {butyrylcholinesterase, catalytic parameters, kinetic models}, title = {Comparison of two reaction schemes for the the hydrolysis of acetylthiocholine by butyrylcholinesterase}, keyword = {butyrylcholinesterase, catalytic parameters, kinetic models}, publisherplace = {St. Moritz, \v{S}vicarska} }




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