Changes in conformation of proteins in solution may be detected by determin ing the relative surface tensions of their solutions. Of the proteins examined, all of the enzymes had distinct changes in surface tensions upon going from a 3M NaCl medium to a salt-free aqueous solution. Only two of the seven non- enzymic proteins underwent detectable changes in the same cycle. These relative surface tensions could be of value in determining adsorption/elution profiles for hydrophobic interaction chromatography.
Get full access to this article
View all access options for this article.
References
1.
(a) Ochoa, J.-L.Biochimie, 60:1 (1978)
2.
; (b) Srinivasan, R. and E. Ruckenstein.Separation and Purification Methods , 9:267 (1980)
3.
; (c) Regnier, F.E.Science, 222:245 (1983).
4.
van Oss, C.J. , D.R. Absolom and A.W. Neumann.Colloid and Polymer Science , 258:424 (1980).
5.
Neumann, A.W. , R.J. Good, C.J. Hope and M. Sejpal.J. Colloid and Interfacial Science , 49:291 (1974).
6.
Handbook of Chemistry and Physics, 47th edition. The Chemical Rubber Co., Cleveland, Ohio, p. F25( 1966).
7.
van Oss, C.J. , A.W. Neumann, S.N. Omemyi and D.R. Absolom.Separation and Purification Methods , 7:245 (1978).
8.
Flory, P.J.Principles of Polymer ChemistryIthaca, NY: Cornell University Press, p. 308 (1953).
9.
Shafrin, E.G. in Polymer Handbook. J. Brandrup and E. H. Immergut, eds. 2ndedition. NY: Interscience, p. III 221.
