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A Radioimmunoassay for the Myelin‐Associated Glycoprotein

A Radioimmunoassay for the Myelin‐Associated Glycoprotein Abstract: The myelin‐associated glycoprotein (MAG) was purified from rat brain and radioiodinated with Bolton‐Hunter reagent for use in a double‐antibody radioimmunoassay. The conditions of the assay were adjusted to measure between 2 and 30 ng of MAG. The antigenic sites of MAG in tissue samples were exposed by solubilization in 1% (wt/vol) sodium dodecyl sulfate (SDS), and the final assay was done in a mixture of 0.25% SDS and 0.25% Triton X‐100. The presence of the Triton X‐100 overcame the inhibitory effect of SDS alone on the immune reactions. Application of the assay to whole homogenates of developing rat brain revealed the expected increase of MAG with the progression of myelination. Adult brain homogenate and purified myelin contained 2.7 and 7.4 μg of MAG/mg protein, respectively. Sciatic nerve contained a lower level of MAG, and cross‐reacting material was not detected in nonneural tissues. This assay makes possible for the first time the analysis of MAG in whole tissue without prior myelin isolation or glycoprotein separation. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Neurochemistry Wiley

A Radioimmunoassay for the Myelin‐Associated Glycoprotein

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References (27)

Publisher
Wiley
Copyright
Copyright © 1982 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0022-3042
eISSN
1471-4159
DOI
10.1111/j.1471-4159.1982.tb12578.x
Publisher site
See Article on Publisher Site

Abstract

Abstract: The myelin‐associated glycoprotein (MAG) was purified from rat brain and radioiodinated with Bolton‐Hunter reagent for use in a double‐antibody radioimmunoassay. The conditions of the assay were adjusted to measure between 2 and 30 ng of MAG. The antigenic sites of MAG in tissue samples were exposed by solubilization in 1% (wt/vol) sodium dodecyl sulfate (SDS), and the final assay was done in a mixture of 0.25% SDS and 0.25% Triton X‐100. The presence of the Triton X‐100 overcame the inhibitory effect of SDS alone on the immune reactions. Application of the assay to whole homogenates of developing rat brain revealed the expected increase of MAG with the progression of myelination. Adult brain homogenate and purified myelin contained 2.7 and 7.4 μg of MAG/mg protein, respectively. Sciatic nerve contained a lower level of MAG, and cross‐reacting material was not detected in nonneural tissues. This assay makes possible for the first time the analysis of MAG in whole tissue without prior myelin isolation or glycoprotein separation.

Journal

Journal of NeurochemistryWiley

Published: Nov 1, 1982

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