A chromatographic method for estimating hydrophobic and electrostatic surface properties of soluble proteins
In this research experiments were carried out to estimate hydrophobic and electrostatic interactions in soluble proteins. Five proteins, lysozyme, lactalbumin, ovalbumin, myoglobin and ribonuclease-A were chromatographed isocratically on a HIC column at several molalities (0.3-1.3m) of each of three...
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| Language: | English |
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University of British Columbia
2010
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| Online Access: | http://hdl.handle.net/2429/29205 |