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Interfacial Rheological and Tension Properties of Protein Films

✍ Scribed by Diane J. Burgess; N.Ozlen Sahin

Publisher
Elsevier Science
Year
1997
Tongue
English
Weight
196 KB
Volume
189
Category
Article
ISSN
0021-9797

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✦ Synopsis

The purpose of this study was to investigate and compare inbulk protein molecules may result as consequences of enviterfacial rheological and tension properties of adsorbed protein ronmental changes, including pH, ionic strength, temperafilms under conditions known to affect bulk properties of proteins. ture, aging, protein concentration, and the addition of certain In previous publications, the effects of pH, protein concentration, chemical agents (3 -5) . Urea, guanidine hydrochloride, and temperature, and aging on the interfacial rheology of bovine serum copper sulfate are examples of protein chemical denaturants albumin (BSA) and human immunoglobulin G (HI g G) were re-( 5) . These molecules bind to proteins, resulting in loss of ported (D.

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