Analysis of toxoplasma gondii proteins after Triton X-114 solubilization and hidropholic chromotograhy
Autor(a) principal: | |
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Data de Publicação: | 1988 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Memórias do Instituto Oswaldo Cruz |
Texto Completo: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02761988000400019 |
Resumo: | The distribution of the surface proteins of toxoplasma gondii radiodinated were studied using the phase separation technique and ability of binding in the phenyl-Sepharose column. Eight polypeptides with Mr 22 to 180 distributed exclusively in the detergent rich-phase, while six polypeptides with mol. wt. 15,000 to 76,000 distributed exclusively in the detergent poor-phase. Twopolypeptides with 15,000 and 70,000 distributed on both phase. All the polypeptides present in the detergent rich-phase binding in the phenyl-Sepharose column, and can be isolated in two peak according with their relative hydrophobicities.two polypeptides hydrophobic with Mr 60 and 66 recognized by human serum were isolated by the association of the two technique. Our result showed that the surface proteins of t. gondii present different degrees of hydrophobicity and that the use of hydrophobic interaction chromatography after Triton X-114 extraction may be an important isolation method of membrane proteins. |
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Memórias do Instituto Oswaldo Cruz |
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Analysis of toxoplasma gondii proteins after Triton X-114 solubilization and hidropholic chromotograhyToxoplasma gondiiTriton X-114hydrophobicitiesmembrane proteinshydrophobic chromatographyThe distribution of the surface proteins of toxoplasma gondii radiodinated were studied using the phase separation technique and ability of binding in the phenyl-Sepharose column. Eight polypeptides with Mr 22 to 180 distributed exclusively in the detergent rich-phase, while six polypeptides with mol. wt. 15,000 to 76,000 distributed exclusively in the detergent poor-phase. Twopolypeptides with 15,000 and 70,000 distributed on both phase. All the polypeptides present in the detergent rich-phase binding in the phenyl-Sepharose column, and can be isolated in two peak according with their relative hydrophobicities.two polypeptides hydrophobic with Mr 60 and 66 recognized by human serum were isolated by the association of the two technique. Our result showed that the surface proteins of t. gondii present different degrees of hydrophobicity and that the use of hydrophobic interaction chromatography after Triton X-114 extraction may be an important isolation method of membrane proteins.Instituto Oswaldo Cruz, Ministério da Saúde1988-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02761988000400019Memórias do Instituto Oswaldo Cruz v.83 n.4 1988reponame:Memórias do Instituto Oswaldo Cruzinstname:Fundação Oswaldo Cruzinstacron:FIOCRUZ10.1590/S0074-02761988000400019info:eu-repo/semantics/openAccessDe Simone,Salvatore GiovanniGuedes,Helena C. B.Bendet,Izidroeng2020-04-25T17:46:09Zhttp://www.scielo.br/oai/scielo-oai.php0074-02761678-8060opendoar:null2020-04-26 02:02:34.071Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruztrue |
dc.title.none.fl_str_mv |
Analysis of toxoplasma gondii proteins after Triton X-114 solubilization and hidropholic chromotograhy |
title |
Analysis of toxoplasma gondii proteins after Triton X-114 solubilization and hidropholic chromotograhy |
spellingShingle |
Analysis of toxoplasma gondii proteins after Triton X-114 solubilization and hidropholic chromotograhy De Simone,Salvatore Giovanni Toxoplasma gondii Triton X-114 hydrophobicities membrane proteins hydrophobic chromatography |
title_short |
Analysis of toxoplasma gondii proteins after Triton X-114 solubilization and hidropholic chromotograhy |
title_full |
Analysis of toxoplasma gondii proteins after Triton X-114 solubilization and hidropholic chromotograhy |
title_fullStr |
Analysis of toxoplasma gondii proteins after Triton X-114 solubilization and hidropholic chromotograhy |
title_full_unstemmed |
Analysis of toxoplasma gondii proteins after Triton X-114 solubilization and hidropholic chromotograhy |
title_sort |
Analysis of toxoplasma gondii proteins after Triton X-114 solubilization and hidropholic chromotograhy |
author |
De Simone,Salvatore Giovanni |
author_facet |
De Simone,Salvatore Giovanni Guedes,Helena C. B. Bendet,Izidro |
author_role |
author |
author2 |
Guedes,Helena C. B. Bendet,Izidro |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
De Simone,Salvatore Giovanni Guedes,Helena C. B. Bendet,Izidro |
dc.subject.por.fl_str_mv |
Toxoplasma gondii Triton X-114 hydrophobicities membrane proteins hydrophobic chromatography |
topic |
Toxoplasma gondii Triton X-114 hydrophobicities membrane proteins hydrophobic chromatography |
dc.description.none.fl_txt_mv |
The distribution of the surface proteins of toxoplasma gondii radiodinated were studied using the phase separation technique and ability of binding in the phenyl-Sepharose column. Eight polypeptides with Mr 22 to 180 distributed exclusively in the detergent rich-phase, while six polypeptides with mol. wt. 15,000 to 76,000 distributed exclusively in the detergent poor-phase. Twopolypeptides with 15,000 and 70,000 distributed on both phase. All the polypeptides present in the detergent rich-phase binding in the phenyl-Sepharose column, and can be isolated in two peak according with their relative hydrophobicities.two polypeptides hydrophobic with Mr 60 and 66 recognized by human serum were isolated by the association of the two technique. Our result showed that the surface proteins of t. gondii present different degrees of hydrophobicity and that the use of hydrophobic interaction chromatography after Triton X-114 extraction may be an important isolation method of membrane proteins. |
description |
The distribution of the surface proteins of toxoplasma gondii radiodinated were studied using the phase separation technique and ability of binding in the phenyl-Sepharose column. Eight polypeptides with Mr 22 to 180 distributed exclusively in the detergent rich-phase, while six polypeptides with mol. wt. 15,000 to 76,000 distributed exclusively in the detergent poor-phase. Twopolypeptides with 15,000 and 70,000 distributed on both phase. All the polypeptides present in the detergent rich-phase binding in the phenyl-Sepharose column, and can be isolated in two peak according with their relative hydrophobicities.two polypeptides hydrophobic with Mr 60 and 66 recognized by human serum were isolated by the association of the two technique. Our result showed that the surface proteins of t. gondii present different degrees of hydrophobicity and that the use of hydrophobic interaction chromatography after Triton X-114 extraction may be an important isolation method of membrane proteins. |
publishDate |
1988 |
dc.date.none.fl_str_mv |
1988-12-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02761988000400019 |
url |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02761988000400019 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0074-02761988000400019 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Instituto Oswaldo Cruz, Ministério da Saúde |
publisher.none.fl_str_mv |
Instituto Oswaldo Cruz, Ministério da Saúde |
dc.source.none.fl_str_mv |
Memórias do Instituto Oswaldo Cruz v.83 n.4 1988 reponame:Memórias do Instituto Oswaldo Cruz instname:Fundação Oswaldo Cruz instacron:FIOCRUZ |
reponame_str |
Memórias do Instituto Oswaldo Cruz |
collection |
Memórias do Instituto Oswaldo Cruz |
instname_str |
Fundação Oswaldo Cruz |
instacron_str |
FIOCRUZ |
institution |
FIOCRUZ |
repository.name.fl_str_mv |
Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruz |
repository.mail.fl_str_mv |
|
_version_ |
1669937652209549312 |