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

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, Norma Lidia, Stella de Rosellini, Ana María Cristina, Batlle, Alcira María del Carmen
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:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v12_n5-6_p745_Bustos http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p745_Bustos
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_0020711X_v12_n5-6_p745_Bustos
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spelling	paper:paper_0020711X_v12_n5-6_p745_Bustos2023-06-08T14:41:03Z Studies on erythrocyte aminolaevulinate dehydratase I. Its purification and possible therapeutic applications Bustos, Norma Lidia Stella de Rosellini, Ana María Cristina Batlle, Alcira María del Carmen 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 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. 1980 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v12_n5-6_p745_Bustos http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p745_Bustos
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (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, Norma Lidia Stella de Rosellini, Ana María Cristina Batlle, Alcira María del Carmen 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.
author	Bustos, Norma Lidia Stella de Rosellini, Ana María Cristina Batlle, Alcira María del Carmen
author_facet	Bustos, Norma Lidia Stella de Rosellini, Ana María Cristina Batlle, Alcira María del Carmen
author_sort	Bustos, Norma Lidia
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	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v12_n5-6_p745_Bustos http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p745_Bustos
work_keys_str_mv	AT bustosnormalidia studiesonerythrocyteaminolaevulinatedehydrataseiitspurificationandpossibletherapeuticapplications AT stelladerosellinianamariacristina studiesonerythrocyteaminolaevulinatedehydrataseiitspurificationandpossibletherapeuticapplications AT batllealciramariadelcarmen studiesonerythrocyteaminolaevulinatedehydrataseiitspurificationandpossibletherapeuticapplications
_version_	1768545538459828224

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

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