Protein purification: adsorption chromatography on controlled pore glass with the use of chaotropic buffers

Science
H G BockS Harshman

Abstract

Chromatography on controlled pore glass in combination with chaotropic buffers makes possible, in a single step, protein purifications of several hundredfold. The new emphasis is on highly selective controllable adsorption. The method is useful for the purification and concentration of proteins from large volumes of complex media and for the purification of proteins that are poorly soluble or tend to aggregate in aqueous solution D-(-)-Beta-Hydroxybutyrate dehydrogenase, a mitochondrial membrane-bound protein, several soluble proteins, and staphylococcal alpha toxin, which can be purified directly from large volumes of culture medium, are used to illustrate the method.

Citations

Sep 12, 1979·Biochimica Et Biophysica Acta·C C HuangM Abramson
Sep 29, 1979·Biochimica Et Biophysica Acta·I A BraudeE de Clercq
Jan 1, 1985·Toxicon : Official Journal of the International Society on Toxinology·J J Lipman, S Harshman
Nov 8, 1996·Journal of Chromatography. a·D H ReifsnyderS E Builder
Jan 1, 1981·Preparative Biochemistry·K C Chadha, E Sulkowski
Aug 1, 1978·Journal of Pharmaceutical Sciences·T Mizutani, A Mizutani
Jul 29, 2004·Biotechnology and Bioengineering·Sanchayita GhoseBrian Hubbard
Jul 15, 1979·Analytical Biochemistry·S Gerard, W M Mitchell
Nov 1, 1977·Analytical Biochemistry·T Mizutani, A Mizutani

Related Concepts

Adsorption
Apoenzymes
Ampholytes
Chromatography
Enterotoxins
Glass (Substance)
Hydrogen-Ion Concentration
3-Hydroxybutyrate Dehydrogenase
Osmolality
Gene Products, Protein

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