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.
|Number of pages||6|
|Journal||European Journal of Biochemistry|
|State||Published - Dec 1973|