Quantification of adsorbed human serum albumin: A comparison between radioimmunoassay and simple null ellipsometry
Autor(a) principal: | |
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Data de Publicação: | 2000 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/1822/13399 |
Resumo: | Radioimmunoassay (RIA) and null ellipsometry are two common methods to quantify adsorbed proteins. However, the accuracy of null ellipsometry with a constant protein refractive index (n 1.465, k 0) at l 632.8 nm has this far not been explored. The present study compared the methods, and the degree of agreement between the simplified single wavelength null ellipsometry and RIA to quantify adsorbed proteins was explored on different surfaces. The quantification methods agreed well when A, ngstro¨m smooth hydrophilic or hydrophobic silicon surfaces, and freshly radio-labelled proteins were used. Some discrepancies were noted when either rough surfaces or stored and aged labelled proteins were used. The differences decreased when the aged protein solution was equilibrated with freshly dissolved proteins at room temperature (RT) for a few hours prior to the surface incubations. Significant differences were also noted between the methods when albumin was adsorbed at it’s iso-electric point (pH 4.8). |
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Quantification of adsorbed human serum albumin: A comparison between radioimmunoassay and simple null ellipsometryRIARadioimmunoassayEllipsometryHuman serum albuminAdsorptionComparisonHydrophilicHydrophobicSiliconRadioimmunoassay (RIA) and null ellipsometry are two common methods to quantify adsorbed proteins. However, the accuracy of null ellipsometry with a constant protein refractive index (n 1.465, k 0) at l 632.8 nm has this far not been explored. The present study compared the methods, and the degree of agreement between the simplified single wavelength null ellipsometry and RIA to quantify adsorbed proteins was explored on different surfaces. The quantification methods agreed well when A, ngstro¨m smooth hydrophilic or hydrophobic silicon surfaces, and freshly radio-labelled proteins were used. Some discrepancies were noted when either rough surfaces or stored and aged labelled proteins were used. The differences decreased when the aged protein solution was equilibrated with freshly dissolved proteins at room temperature (RT) for a few hours prior to the surface incubations. Significant differences were also noted between the methods when albumin was adsorbed at it’s iso-electric point (pH 4.8).Universidade do MinhoBenesch, JohanAskendal, A.Tengvall, P.20002000-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/13399enginfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-21T12:38:31Zoai:repositorium.sdum.uminho.pt:1822/13399Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:35:00.069852Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Quantification of adsorbed human serum albumin: A comparison between radioimmunoassay and simple null ellipsometry |
title |
Quantification of adsorbed human serum albumin: A comparison between radioimmunoassay and simple null ellipsometry |
spellingShingle |
Quantification of adsorbed human serum albumin: A comparison between radioimmunoassay and simple null ellipsometry Benesch, Johan RIA Radioimmunoassay Ellipsometry Human serum albumin Adsorption Comparison Hydrophilic Hydrophobic Silicon |
title_short |
Quantification of adsorbed human serum albumin: A comparison between radioimmunoassay and simple null ellipsometry |
title_full |
Quantification of adsorbed human serum albumin: A comparison between radioimmunoassay and simple null ellipsometry |
title_fullStr |
Quantification of adsorbed human serum albumin: A comparison between radioimmunoassay and simple null ellipsometry |
title_full_unstemmed |
Quantification of adsorbed human serum albumin: A comparison between radioimmunoassay and simple null ellipsometry |
title_sort |
Quantification of adsorbed human serum albumin: A comparison between radioimmunoassay and simple null ellipsometry |
author |
Benesch, Johan |
author_facet |
Benesch, Johan Askendal, A. Tengvall, P. |
author_role |
author |
author2 |
Askendal, A. Tengvall, P. |
author2_role |
author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Benesch, Johan Askendal, A. Tengvall, P. |
dc.subject.por.fl_str_mv |
RIA Radioimmunoassay Ellipsometry Human serum albumin Adsorption Comparison Hydrophilic Hydrophobic Silicon |
topic |
RIA Radioimmunoassay Ellipsometry Human serum albumin Adsorption Comparison Hydrophilic Hydrophobic Silicon |
description |
Radioimmunoassay (RIA) and null ellipsometry are two common methods to quantify adsorbed proteins. However, the accuracy of null ellipsometry with a constant protein refractive index (n 1.465, k 0) at l 632.8 nm has this far not been explored. The present study compared the methods, and the degree of agreement between the simplified single wavelength null ellipsometry and RIA to quantify adsorbed proteins was explored on different surfaces. The quantification methods agreed well when A, ngstro¨m smooth hydrophilic or hydrophobic silicon surfaces, and freshly radio-labelled proteins were used. Some discrepancies were noted when either rough surfaces or stored and aged labelled proteins were used. The differences decreased when the aged protein solution was equilibrated with freshly dissolved proteins at room temperature (RT) for a few hours prior to the surface incubations. Significant differences were also noted between the methods when albumin was adsorbed at it’s iso-electric point (pH 4.8). |
publishDate |
2000 |
dc.date.none.fl_str_mv |
2000 2000-01-01T00:00:00Z |
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://hdl.handle.net/1822/13399 |
url |
http://hdl.handle.net/1822/13399 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
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1799132873551249408 |