Effect of crowding by Dextrans in enzymatic reactions

The interior of the living cell is highly concentrated and structured with molecules that have different shapes and sizes. Almost all experimental biochemical data have been obtained working in dilute solutions, situations which do not reflect the in vivo conditions. The consequences of such crowdin...

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Autores: Pastor, Isabel, Balcells Nadal, Cristina, Pitulice, Laura, Vilaseca i Font, Eudald, Madurga Díez, Sergio, Isvoran, Adriana, Cascante i Serratosa, Marta, Mas i Pujadas, Francesc
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2014
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/104310
Acceso en línea:https://hdl.handle.net/2445/104310
Access Level:acceso abierto
Palabra clave:Cinètica enzimàtica
Macromolècules
Enzyme kinetics
Macromolecules
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spelling Effect of crowding by Dextrans in enzymatic reactionsPastor, IsabelBalcells Nadal, CristinaPitulice, LauraVilaseca i Font, EudaldMadurga Díez, SergioIsvoran, AdrianaCascante i Serratosa, MartaMas i Pujadas, FrancescCinètica enzimàticaMacromolèculesEnzyme kineticsMacromoleculesThe interior of the living cell is highly concentrated and structured with molecules that have different shapes and sizes. Almost all experimental biochemical data have been obtained working in dilute solutions, situations which do not reflect the in vivo conditions. The consequences of such crowding upon enzymatic reactions remain unclear. In this paper, we have studied and compared the initial velocity of the hydrolysis of N-succinyl-l-phenyl-Ala-p-nitroanilide catalyzed by alpha-chymotrypsin, the oxidation of ABTS by H2O2 catalyzed by HRP and the oxidation of NADH in presence of pyruvate catalyzed by LDH. These reactions were chosen as model enzymatic processes occurring in different in vitro crowded media. The systems crowding has been built by introducing Dextran of several concentrations and sizes. Our results indicate that the volume occupied by the crowding agent, but not its size, plays an important role on the initial velocity of reactions involving tiny enzymes. However, the enzyme size is another important factor influencing the velocity of the reactions of large enzymes occurring in Dextran crowded media. In this situation, the reaction initial velocity depends on both occupied volume and dimension of the crowding agent that is present in the reaction media.Elsevier B.V.2016201620142016info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersion6 p.application/pdfhttps://hdl.handle.net/2445/104310Articles publicats en revistes (Ciència dels Materials i Química Física)reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésVersió postprint del document publicat a: https://doi.org/10.1016/j.bpc.2013.10.006Biophysical Chemistry, 2014, vol. 185, p. 8-13https://doi.org/10.1016/j.bpc.2013.10.006(c) Elsevier B.V., 2014info:eu-repo/semantics/openAccessoai:recercat.cat:2445/1043102026-05-29T05:05:01Z
dc.title.none.fl_str_mv Effect of crowding by Dextrans in enzymatic reactions
title Effect of crowding by Dextrans in enzymatic reactions
spellingShingle Effect of crowding by Dextrans in enzymatic reactions
Pastor, Isabel
Cinètica enzimàtica
Macromolècules
Enzyme kinetics
Macromolecules
title_short Effect of crowding by Dextrans in enzymatic reactions
title_full Effect of crowding by Dextrans in enzymatic reactions
title_fullStr Effect of crowding by Dextrans in enzymatic reactions
title_full_unstemmed Effect of crowding by Dextrans in enzymatic reactions
title_sort Effect of crowding by Dextrans in enzymatic reactions
dc.creator.none.fl_str_mv Pastor, Isabel
Balcells Nadal, Cristina
Pitulice, Laura
Vilaseca i Font, Eudald
Madurga Díez, Sergio
Isvoran, Adriana
Cascante i Serratosa, Marta
Mas i Pujadas, Francesc
author Pastor, Isabel
author_facet Pastor, Isabel
Balcells Nadal, Cristina
Pitulice, Laura
Vilaseca i Font, Eudald
Madurga Díez, Sergio
Isvoran, Adriana
Cascante i Serratosa, Marta
Mas i Pujadas, Francesc
author_role author
author2 Balcells Nadal, Cristina
Pitulice, Laura
Vilaseca i Font, Eudald
Madurga Díez, Sergio
Isvoran, Adriana
Cascante i Serratosa, Marta
Mas i Pujadas, Francesc
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Cinètica enzimàtica
Macromolècules
Enzyme kinetics
Macromolecules
topic Cinètica enzimàtica
Macromolècules
Enzyme kinetics
Macromolecules
description The interior of the living cell is highly concentrated and structured with molecules that have different shapes and sizes. Almost all experimental biochemical data have been obtained working in dilute solutions, situations which do not reflect the in vivo conditions. The consequences of such crowding upon enzymatic reactions remain unclear. In this paper, we have studied and compared the initial velocity of the hydrolysis of N-succinyl-l-phenyl-Ala-p-nitroanilide catalyzed by alpha-chymotrypsin, the oxidation of ABTS by H2O2 catalyzed by HRP and the oxidation of NADH in presence of pyruvate catalyzed by LDH. These reactions were chosen as model enzymatic processes occurring in different in vitro crowded media. The systems crowding has been built by introducing Dextran of several concentrations and sizes. Our results indicate that the volume occupied by the crowding agent, but not its size, plays an important role on the initial velocity of reactions involving tiny enzymes. However, the enzyme size is another important factor influencing the velocity of the reactions of large enzymes occurring in Dextran crowded media. In this situation, the reaction initial velocity depends on both occupied volume and dimension of the crowding agent that is present in the reaction media.
publishDate 2014
dc.date.none.fl_str_mv 2014
2016
2016
2016
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/104310
url https://hdl.handle.net/2445/104310
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Versió postprint del document publicat a: https://doi.org/10.1016/j.bpc.2013.10.006
Biophysical Chemistry, 2014, vol. 185, p. 8-13
https://doi.org/10.1016/j.bpc.2013.10.006
dc.rights.none.fl_str_mv (c) Elsevier B.V., 2014
info:eu-repo/semantics/openAccess
rights_invalid_str_mv (c) Elsevier B.V., 2014
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 6 p.
application/pdf
dc.publisher.none.fl_str_mv Elsevier B.V.
publisher.none.fl_str_mv Elsevier B.V.
dc.source.none.fl_str_mv Articles publicats en revistes (Ciència dels Materials i Química Física)
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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