The adverse effect of neuraminidase on the analysis of cell surfaces by borohydride tritiation

Many techniques have been developed to label surface components of cell membranes. One is the galactose oxidase/sodium borohydride procedure where terminal galactose or N-acetylgalactosamine residues of carbohydrate chains are first oxidised by galactose oxidase then tritiated by reduction with NaB...

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Bibliographic Details
Published in:FEBS letters 1981-10, Vol.133 (1), p.165-168
Main Authors: Thompson, S., Maddy, A.H.
Format: Article
Language:English
Subjects:
Adult
Borohydrides
carbohydrates
cell surface
Electrophoresis, Polyacrylamide Gel
Erythrocyte Membrane - analysis
Erythrocyte Membrane - drug effects
erythrocytes
Erythrocytes - analysis
Female
Galactose Oxidase
Glycoproteins - blood
Humans
Male
methodology
neuraminidase
Neuraminidase - pharmacology
Oxidation-Reduction
sodium borhydride
Tritium
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Summary:Many techniques have been developed to label surface components of cell membranes. One is the galactose oxidase/sodium borohydride procedure where terminal galactose or N-acetylgalactosamine residues of carbohydrate chains are first oxidised by galactose oxidase then tritiated by reduction with NaB super(3)H sub(4). In this method neuraminidase is almost invariably added along with the galactose oxidase as the removal of sialic acid increases the number of terminal galactose residues and hence the uptake of tritium on reduction. Using the erythrocyte surface as a model, the authors find that neuraminidase treatment has a deleterious effect on the mobility and resolution of labelled glycoproteins in sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis (PAGE). They suggest that this undesirable consequence of neuraminidase needs to be carefully considered when the enzyme is used to enhance galactose oxidase/borohydride tritiation of cell surfaces.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(81)80496-6