Development of HPLC methods for the purification and analysis of plasma membrane glycoproteins.

High resolution HPLC techniques such as affinity chromatography (AC), ion exchange chromatography (IEC), and size exclusion chromatography (SEC) were used successfully for separations of hydrophobic plasma membrane glycoproteins. We have tested a lot of commercially available columns for IEC and SEC...

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Detalles Bibliográficos
Autores principales: Renauer, D, Gierlich, H U, Unger, K K
Formato: Texto
Lenguaje:English
Publicado: 1990
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1568031/
https://www.ncbi.nlm.nih.gov/pubmed/2272317
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author Renauer, D
Gierlich, H U
Unger, K K
author_facet Renauer, D
Gierlich, H U
Unger, K K
author_sort Renauer, D
collection PubMed
description High resolution HPLC techniques such as affinity chromatography (AC), ion exchange chromatography (IEC), and size exclusion chromatography (SEC) were used successfully for separations of hydrophobic plasma membrane glycoproteins. We have tested a lot of commercially available columns for IEC and SEC and performed the purification of the crude plasma membrane extract with the most suitable columns. By using immobilized ligands with different specificities and sequential affinity chromatography, it is possible to obtain a preliminary structural characterization of the interesting carbohydrate residues of membrane glycoproteins.
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spelling pubmed-15680312006-09-18 Development of HPLC methods for the purification and analysis of plasma membrane glycoproteins. Renauer, D Gierlich, H U Unger, K K Environ Health Perspect Research Article High resolution HPLC techniques such as affinity chromatography (AC), ion exchange chromatography (IEC), and size exclusion chromatography (SEC) were used successfully for separations of hydrophobic plasma membrane glycoproteins. We have tested a lot of commercially available columns for IEC and SEC and performed the purification of the crude plasma membrane extract with the most suitable columns. By using immobilized ligands with different specificities and sequential affinity chromatography, it is possible to obtain a preliminary structural characterization of the interesting carbohydrate residues of membrane glycoproteins. 1990-08 /pmc/articles/PMC1568031/ /pubmed/2272317 Text en
spellingShingle Research Article
Renauer, D
Gierlich, H U
Unger, K K
Development of HPLC methods for the purification and analysis of plasma membrane glycoproteins.
title Development of HPLC methods for the purification and analysis of plasma membrane glycoproteins.
title_full Development of HPLC methods for the purification and analysis of plasma membrane glycoproteins.
title_fullStr Development of HPLC methods for the purification and analysis of plasma membrane glycoproteins.
title_full_unstemmed Development of HPLC methods for the purification and analysis of plasma membrane glycoproteins.
title_short Development of HPLC methods for the purification and analysis of plasma membrane glycoproteins.
title_sort development of hplc methods for the purification and analysis of plasma membrane glycoproteins.
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1568031/
https://www.ncbi.nlm.nih.gov/pubmed/2272317
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AT gierlichhu developmentofhplcmethodsforthepurificationandanalysisofplasmamembraneglycoproteins
AT ungerkk developmentofhplcmethodsforthepurificationandanalysisofplasmamembraneglycoproteins

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