Solubilization of membrane-bound matrix-induced alkaline phosphatase with polyoxyethylene 9-lauryl ether (polidocanol): Purification and metalloenzyme properties
Autor(a) principal: | |
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Data de Publicação: | 1990 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1016/0020-711X(90)90141-O http://hdl.handle.net/11449/223916 |
Resumo: | 1. 1. Matrix-induced alkaline phosphatase prepared from rat osseous plate was solubilized with polidocanol and purified on a Sephacryl S-300 column. 2. 2. Purified solubilized alkaline phosphatase has a molecular weight of ca 115,000 and bind one magnesium and two zinc ions. At least 110 detergent molecules are bound to each enzyme molecule. 3. 3. Solubilization and purification procedures did not destroy the ability of the enzyme to hydrolyze adenosine-5'-triphosphate, p-nitrophenylphosphate, pyrophosphate and bis p-nitrophenylphosphate. 4. 4. Magnesium, manganese and cobalt ions are stimulators of PNPPase activity of solubilized enzyme whereas calcium and zinc ions are inhibitors. © 1990. |
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Solubilization of membrane-bound matrix-induced alkaline phosphatase with polyoxyethylene 9-lauryl ether (polidocanol): Purification and metalloenzyme properties1. 1. Matrix-induced alkaline phosphatase prepared from rat osseous plate was solubilized with polidocanol and purified on a Sephacryl S-300 column. 2. 2. Purified solubilized alkaline phosphatase has a molecular weight of ca 115,000 and bind one magnesium and two zinc ions. At least 110 detergent molecules are bound to each enzyme molecule. 3. 3. Solubilization and purification procedures did not destroy the ability of the enzyme to hydrolyze adenosine-5'-triphosphate, p-nitrophenylphosphate, pyrophosphate and bis p-nitrophenylphosphate. 4. 4. Magnesium, manganese and cobalt ions are stimulators of PNPPase activity of solubilized enzyme whereas calcium and zinc ions are inhibitors. © 1990.Departamento de Química, Faculdade de Filosofia, Ciências e Letras-USP, 14049 Ribeirão Preto, SPDepartamento de Tecnologia, Faculdade de Ciências Agrárias e Veterinárias-UNESP., 14870 Jaboticabal, SPDepartamento de Tecnologia, Faculdade de Ciências Agrárias e Veterinárias-UNESP., 14870 Jaboticabal, SPUniversidade de São Paulo (USP)Universidade Estadual Paulista (UNESP)Ciancaglini, P.Pizauro, J. M. [UNESP]Rezende, A. A.Rezende, L. A.Leone, F. A.2022-04-28T19:53:48Z2022-04-28T19:53:48Z1990-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article385-392http://dx.doi.org/10.1016/0020-711X(90)90141-OInternational Journal of Biochemistry, v. 22, n. 4, p. 385-392, 1990.0020-711Xhttp://hdl.handle.net/11449/22391610.1016/0020-711X(90)90141-O2-s2.0-0025248892Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengInternational Journal of Biochemistryinfo:eu-repo/semantics/openAccess2022-04-28T19:53:48Zoai:repositorio.unesp.br:11449/223916Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462022-04-28T19:53:48Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Solubilization of membrane-bound matrix-induced alkaline phosphatase with polyoxyethylene 9-lauryl ether (polidocanol): Purification and metalloenzyme properties |
title |
Solubilization of membrane-bound matrix-induced alkaline phosphatase with polyoxyethylene 9-lauryl ether (polidocanol): Purification and metalloenzyme properties |
spellingShingle |
Solubilization of membrane-bound matrix-induced alkaline phosphatase with polyoxyethylene 9-lauryl ether (polidocanol): Purification and metalloenzyme properties Ciancaglini, P. |
title_short |
Solubilization of membrane-bound matrix-induced alkaline phosphatase with polyoxyethylene 9-lauryl ether (polidocanol): Purification and metalloenzyme properties |
title_full |
Solubilization of membrane-bound matrix-induced alkaline phosphatase with polyoxyethylene 9-lauryl ether (polidocanol): Purification and metalloenzyme properties |
title_fullStr |
Solubilization of membrane-bound matrix-induced alkaline phosphatase with polyoxyethylene 9-lauryl ether (polidocanol): Purification and metalloenzyme properties |
title_full_unstemmed |
Solubilization of membrane-bound matrix-induced alkaline phosphatase with polyoxyethylene 9-lauryl ether (polidocanol): Purification and metalloenzyme properties |
title_sort |
Solubilization of membrane-bound matrix-induced alkaline phosphatase with polyoxyethylene 9-lauryl ether (polidocanol): Purification and metalloenzyme properties |
author |
Ciancaglini, P. |
author_facet |
Ciancaglini, P. Pizauro, J. M. [UNESP] Rezende, A. A. Rezende, L. A. Leone, F. A. |
author_role |
author |
author2 |
Pizauro, J. M. [UNESP] Rezende, A. A. Rezende, L. A. Leone, F. A. |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Universidade de São Paulo (USP) Universidade Estadual Paulista (UNESP) |
dc.contributor.author.fl_str_mv |
Ciancaglini, P. Pizauro, J. M. [UNESP] Rezende, A. A. Rezende, L. A. Leone, F. A. |
description |
1. 1. Matrix-induced alkaline phosphatase prepared from rat osseous plate was solubilized with polidocanol and purified on a Sephacryl S-300 column. 2. 2. Purified solubilized alkaline phosphatase has a molecular weight of ca 115,000 and bind one magnesium and two zinc ions. At least 110 detergent molecules are bound to each enzyme molecule. 3. 3. Solubilization and purification procedures did not destroy the ability of the enzyme to hydrolyze adenosine-5'-triphosphate, p-nitrophenylphosphate, pyrophosphate and bis p-nitrophenylphosphate. 4. 4. Magnesium, manganese and cobalt ions are stimulators of PNPPase activity of solubilized enzyme whereas calcium and zinc ions are inhibitors. © 1990. |
publishDate |
1990 |
dc.date.none.fl_str_mv |
1990-01-01 2022-04-28T19:53:48Z 2022-04-28T19:53:48Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1016/0020-711X(90)90141-O International Journal of Biochemistry, v. 22, n. 4, p. 385-392, 1990. 0020-711X http://hdl.handle.net/11449/223916 10.1016/0020-711X(90)90141-O 2-s2.0-0025248892 |
url |
http://dx.doi.org/10.1016/0020-711X(90)90141-O http://hdl.handle.net/11449/223916 |
identifier_str_mv |
International Journal of Biochemistry, v. 22, n. 4, p. 385-392, 1990. 0020-711X 10.1016/0020-711X(90)90141-O 2-s2.0-0025248892 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
International Journal of Biochemistry |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
385-392 |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1797789677977075712 |