Thiophilic interaction chromatography of serum albumins.

An investigation of the binding of native and recombinant human serum albumin and bovine serum albumin on three thiophilic gels, PyS, 2S, and 3S was performed. In addition to these proteins, we studied serum albumins from several species such as goat, rabbit, guinea pig, rat, hamster, baboon, and pig. Our results reveal that recombinant human serum albumin (rHSA) binds completely to PyS whereas native human serum albumin and bovine serum albumin bind only partially to PyS.

Thiophilic interaction chromatography of mammalian and avian transferrins.

Transferrins are a class of iron-binding proteins widely distributed in biological fluids. All transferrins possess two metal binding sites, each of which can bind a ferric iron. Transferrins play a major role in plasma iron transport and have anti-bacterial, anti-inflammatory, and immunological functions.

Thiophilic interaction chromatography of human transferrins.

Lactoferrin and serum transferrin, the iron-binding proteins, are widely distributed in biological fluids. Transferrins have many biological functions: anti-bacterial, anti-inflammatory, and immunoregulatory. A facile monitoring of the concentration of transferrins in biological fluids may have medical relevance.