Possible pitfalls in the identification of glycophorin-binding proteins of Plasmodium falciparum.

Plasmodium falciparum proteins that bind to the putative erythrocyte receptor (glycophorin) have been identified in several laboratories by their ability to bind to glycophorin immobilized on aminoethyl-BioGel (AE-BioGel). We here report that several parasite proteins bind to AE-BioGel in the absenc...

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Main Authors: van Schravendijk, MR, Wilson, R, Newbold, C
Format: Journal article
Language:English
Published: 1987
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author van Schravendijk, MR
Wilson, R
Newbold, C
author_facet van Schravendijk, MR
Wilson, R
Newbold, C
author_sort van Schravendijk, MR
collection OXFORD
description Plasmodium falciparum proteins that bind to the putative erythrocyte receptor (glycophorin) have been identified in several laboratories by their ability to bind to glycophorin immobilized on aminoethyl-BioGel (AE-BioGel). We here report that several parasite proteins bind to AE-BioGel in the absence of coupled glycophorin. Binding is apparently due to the strong ion-exchange properties of the matrix, and is sensitive to ionic conditions such as the degree of equilibration of the matrix and the pH. The parasite proteins that bind to the blank column under appropriate conditions include proteins with the serological activities of S-antigen and Ag 23, which also bind to glycophorin-coupled AE-BioGel. In the light of these results, the glycophorin-binding specificity of these and other proteins reported to bind to glycophorin-coupled AE-BioGel will have to be reevaluated, preferably using a different support matrix.
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spelling oxford-uuid:4e0dc6f5-fa2c-46a4-80d4-21c1d52934442022-03-26T15:59:00ZPossible pitfalls in the identification of glycophorin-binding proteins of Plasmodium falciparum.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:4e0dc6f5-fa2c-46a4-80d4-21c1d5293444EnglishSymplectic Elements at Oxford1987van Schravendijk, MRWilson, RNewbold, CPlasmodium falciparum proteins that bind to the putative erythrocyte receptor (glycophorin) have been identified in several laboratories by their ability to bind to glycophorin immobilized on aminoethyl-BioGel (AE-BioGel). We here report that several parasite proteins bind to AE-BioGel in the absence of coupled glycophorin. Binding is apparently due to the strong ion-exchange properties of the matrix, and is sensitive to ionic conditions such as the degree of equilibration of the matrix and the pH. The parasite proteins that bind to the blank column under appropriate conditions include proteins with the serological activities of S-antigen and Ag 23, which also bind to glycophorin-coupled AE-BioGel. In the light of these results, the glycophorin-binding specificity of these and other proteins reported to bind to glycophorin-coupled AE-BioGel will have to be reevaluated, preferably using a different support matrix.
spellingShingle van Schravendijk, MR
Wilson, R
Newbold, C
Possible pitfalls in the identification of glycophorin-binding proteins of Plasmodium falciparum.
title Possible pitfalls in the identification of glycophorin-binding proteins of Plasmodium falciparum.
title_full Possible pitfalls in the identification of glycophorin-binding proteins of Plasmodium falciparum.
title_fullStr Possible pitfalls in the identification of glycophorin-binding proteins of Plasmodium falciparum.
title_full_unstemmed Possible pitfalls in the identification of glycophorin-binding proteins of Plasmodium falciparum.
title_short Possible pitfalls in the identification of glycophorin-binding proteins of Plasmodium falciparum.
title_sort possible pitfalls in the identification of glycophorin binding proteins of plasmodium falciparum
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