A novel chromatographic media: Histidine-containing composite cryogels for HIgG separation from human serum

WOS: 000366797800019PubMed: 25749958Histidine-containing microspheres (HCM) with 2 mu m in size were synthesized by suspension polymerization of poly(hydroxyethyl methacrylate) and N-methacryloyl-L-histidine methyl ester. Then, they were used to prepare composite cryogel columns by an embedding process for affinity depletion of immunoglobulin G (HIgG) from human serum via histidine groups on microspheres. Here, we describe HIgG adsorption performance of composite cryogel columns in both aqueous solution and human serum

Molecularly Imprinted Supermacroporous Cryogels for Myoglobin Recognition

Myoglobin is a primary iron, and oxygen-binding protein of muscle tissues and levels can be an important diagnostic biomarker for acute myocardial infarction, myocardial necrosis, or other cardiac diseases. The establishment of myoglobin recognition systems is important because of its protein's structural and functional values in physiology, biochemistry, and diagnostic value in some damaged muscle tissue and cardiac diseases. For this purpose, we used molecular imprinting technique for myoglobin recognition from aqueous solutions and human plasma. In the first step, myoglobin-imprinted poly(hydroxyethyl methacrylate) (PHEMA) cryogels (MGb-MIP) were prepared, and optimum myoglobin adsorption conditions were determined. Selectivity experiments have been done with the competitive proteins, and myoglobin adsorption from IgG and albumin-free human plasma was studied. The purity of the desorbed samples was determined with SDS-PAGE. The desorption efficiency and reusability of the MGb-MIP cryogels were tested, and it was shown that without any significant loss in the adsorption capacity, MGb-MIP cryogels can be used a number of times for myoglobin recognition and separation