Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications

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1. 1. A method for purifying human erythrocytes ALA-D, using a mixture of n-butanol and chloroform, which denature hemoglobin, followed by ammonium sulphate fractionation and affinity chromatography yielding a 1600-fold purified enzyme, is described. 2. 2. By oxidation of Sephadex G-25 with NaIO4, a...

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Autores principales: Bustos, N., Stella, A.M., Xifra, E.A.W.D., C. Batlle, A.M.D.
Formato: Artículo publishedVersion
Publicado: 1980
Materias:
butanol
chloroform
porphobilinogen synthase
blood and hemopoietic system
enzyme purification
erythrocyte
human cell
in vitro study
normal human
preliminary communication
Enzymes, Immobilized
Erythrocytes
Human
Porphobilinogen Synthase
Support, Non-U.S. Gov't
Thiosulfate Sulfurtransferase
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p745_Bustos
https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_0020711X_v12_n5-6_p745_Bustos_oai
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Repositorio Digital de la Universidad de Buenos Aires (UBA) de Universidad de Buenos Aires
id I28-R145-paper_0020711X_v12_n5-6_p745_Bustos_oai
record_format dspace
spelling I28-R145-paper_0020711X_v12_n5-6_p745_Bustos_oai2024-08-16 Bustos, N. Stella, A.M. Xifra, E.A.W.D. C. Batlle, A.M.D. 1980 1. 1. A method for purifying human erythrocytes ALA-D, using a mixture of n-butanol and chloroform, which denature hemoglobin, followed by ammonium sulphate fractionation and affinity chromatography yielding a 1600-fold purified enzyme, is described. 2. 2. By oxidation of Sephadex G-25 with NaIO4, a polyaldehyde, is obtained which can be covalently bound to the ALA-D; however the immobilized enzyme is inactive, because essential ε{lunate}-amino groups at the active site were involved in the coupling. Similar experiments with another enzyme, Rhodanese, resulted in an active insolubilized preparation. 3. 3. By suspending the carrier-enzyme in buffer, slow solubilization with simultaneous release of protein occurs, indicating that this approach might find important therapeutical applications in the treatment of enzyme deficiencies. © 1980. Fil:Bustos, N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Stella, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:C. Batlle, A.M.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. application/pdf http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p745_Bustos info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar Int. J. Biochem. 1980;12(5-6):745-749 butanol chloroform porphobilinogen synthase blood and hemopoietic system enzyme purification erythrocyte human cell in vitro study normal human preliminary communication Enzymes, Immobilized Erythrocytes Human Porphobilinogen Synthase Support, Non-U.S. Gov't Thiosulfate Sulfurtransferase Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_0020711X_v12_n5-6_p745_Bustos_oai
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-145
collection Repositorio Digital de la Universidad de Buenos Aires (UBA)
topic butanol
chloroform
porphobilinogen synthase
blood and hemopoietic system
enzyme purification
erythrocyte
human cell
in vitro study
normal human
preliminary communication
Enzymes, Immobilized
Erythrocytes
Human
Porphobilinogen Synthase
Support, Non-U.S. Gov't
Thiosulfate Sulfurtransferase
spellingShingle butanol
chloroform
porphobilinogen synthase
blood and hemopoietic system
enzyme purification
erythrocyte
human cell
in vitro study
normal human
preliminary communication
Enzymes, Immobilized
Erythrocytes
Human
Porphobilinogen Synthase
Support, Non-U.S. Gov't
Thiosulfate Sulfurtransferase
Bustos, N.
Stella, A.M.
Xifra, E.A.W.D.
C. Batlle, A.M.D.
Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications
topic_facet butanol
chloroform
porphobilinogen synthase
blood and hemopoietic system
enzyme purification
erythrocyte
human cell
in vitro study
normal human
preliminary communication
Enzymes, Immobilized
Erythrocytes
Human
Porphobilinogen Synthase
Support, Non-U.S. Gov't
Thiosulfate Sulfurtransferase
description 1. 1. A method for purifying human erythrocytes ALA-D, using a mixture of n-butanol and chloroform, which denature hemoglobin, followed by ammonium sulphate fractionation and affinity chromatography yielding a 1600-fold purified enzyme, is described. 2. 2. By oxidation of Sephadex G-25 with NaIO4, a polyaldehyde, is obtained which can be covalently bound to the ALA-D; however the immobilized enzyme is inactive, because essential ε{lunate}-amino groups at the active site were involved in the coupling. Similar experiments with another enzyme, Rhodanese, resulted in an active insolubilized preparation. 3. 3. By suspending the carrier-enzyme in buffer, slow solubilization with simultaneous release of protein occurs, indicating that this approach might find important therapeutical applications in the treatment of enzyme deficiencies. © 1980.
format Artículo
Artículo
publishedVersion
author Bustos, N.
Stella, A.M.
Xifra, E.A.W.D.
C. Batlle, A.M.D.
author_facet Bustos, N.
Stella, A.M.
Xifra, E.A.W.D.
C. Batlle, A.M.D.
author_sort Bustos, N.
title Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications
title_short Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications
title_full Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications
title_fullStr Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications
title_full_unstemmed Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications
title_sort studies on erythrocyte aminolaevulinate dehydratase i. its purification and possible therapeutic applications
publishDate 1980
url http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p745_Bustos
https://repositoriouba.sisbi.uba.ar/gsdl/cgi-bin/library.cgi?a=d&c=artiaex&d=paper_0020711X_v12_n5-6_p745_Bustos_oai
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AT stellaam studiesonerythrocyteaminolaevulinatedehydrataseiitspurificationandpossibletherapeuticapplications
AT xifraeawd studiesonerythrocyteaminolaevulinatedehydrataseiitspurificationandpossibletherapeuticapplications
AT cbatlleamd studiesonerythrocyteaminolaevulinatedehydrataseiitspurificationandpossibletherapeuticapplications
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