Abstract
In this work, we have used Stöber method to prepare 200 nm SiO 2 particles and then immobilized metal affinity ligand iminodiacetic acid (IDA) and charged them with Ni 2+ ions. The particles show high absorption efficiency to bovine hemoglobin and the maximum extraction amounts reached 43.4 mg/g. The particles have been applied to separate a model protein mixture of bovine hemoglobin (BHb) and bovine serum albumin (BSA). They can be separated and showed low non-specific adsorption. Then we have used these particles to extract BHb from the mixture of BHb and DNA. They have potential applications in removing abundant protein in proteomic analysis, and we hope it may become a simple, convenient, and potentially effective way to purify hemoglobin in serum.
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