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Science 30 January 1976:
Vol. 191. no. 4225, pp. 380 - 383
DOI: 10.1126/science.1859
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Articles

Science, Vol 191, Issue 4225, 380-383
Copyright © 1976 by American Association for the Advancement of Science

articles

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

HG Bock, P Skene, S Fleischer, P Cassidy, and S Harshman

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.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Liquid Chromatography in 1982.
D. H. Freeman and D. H. Freeman (1982)
Science 218, 235-241
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