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Abstract
Biopolymers, such as proteins and nucleic acids, were separated by adsorption chromatography on porous glass or siliconized porous glass. The adsorption of proteins on porous glass was caused by two factors; one is amine-silanol ionic bonding and the other is a cooperative aggregative force between silica and proteins. The amount, of proteins and the constituents was approximately 5μmol/g porous glass. Proteins adsorbed on porous glass were separated by exchange of buffers different in kind. Several examples of protein separation on porous glass were shown and the eluting conditions were discussed. Proteins, adsorbed on siliconized porous glass in a high salt solution, were eluted with a low salt solution or with detergents. Nucleic acids, such as tRNA, rRNA and DNA were adsorbed at high concentrations of salt on porous glass or siliconized glass, and separated with a gradient from a high salt solution to a low salt solution with good recovery. Siliconized porous glass was further coated with Adogen 464 and used an identical adsorbent with RPC-5 to separate tRNA species.