Open AccessThe Interaction of Chaotropic Anions with Proteins at Acid pH
Author(s) -
Aviram Irit
Publication year - 1973
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1973.tb03235.x
Subject(s) - chaotropic agent , circular dichroism , chemistry , bovine serum albumin , pepsin , lysozyme , fluorescence , hydrolysis , serum albumin , hemoglobin , biochemistry , crystallography , enzyme , physics , quantum mechanics
The activity of pepsin on small substrates, as well as its autodigestibility, fluorescence and circular dichroism were unaffected by the presence of “disordering” anions. Pepsin activity on hemoglobin and bovine serum albumin was inhibited by the same anions, while the hydrolysis of lysozyme was enhanced. The anions also altered the fluorescence and circular dichroism spectra of bovine serum albumin. These findings are discussed in relation to conformational changes induced by disordering ions at acid pH.