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Abstract : |
Alzheimer`s amyloid أƒإ½أ‚آ²A4 protein fused with glutathione S-transferase (GST) was highly expressed using a strong prokaryotic expression system in Escherichia coli. The expressed protein had expected molecular mass on SDS-PAGE and appeared exclusively immunoreactive with antibody specific for أƒإ½أ‚آ²A4 epitope. This recombinant protein was purified with a combination of urea solubilization and ion exchange chromatography. To identify the human serum proteins which interact with أƒإ½أ‚آ²A4, affinity columns were prepared by immobilizing GST- أƒإ½أ‚آ²A4 and GST respectively. Using the affinity columns and human serum, we have observed an interaction of أƒإ½أ‚آ²A4 with serum proteins. Two proteins of Mr 45 and 15 kDa were identified on SDS-PAGE to be involved in the interaction. Our demonstration of the ability of أƒإ½أ‚آ²A4 to interact with serum protein strongly support the notion that such an interaction may underlie with the biological function of أƒإ½أ‚آ²A4 in vivo., |
