The in vitro effect of Al3þ ions in the concentration range 1.7·1026M–8.7·1023M on pepsin activity at pH 2, via kinetic parameters and its electrophoretic mobility was evaluated. Kinetic study demonstrated the existence of an activation effect of Al3þ at pH 2 on pepsin molecule. Kinetic analysis with respect to concentrations of haemoglobin showed that Al3þ ions increase the maximal velocity (Vmax) and kcat values rather than apparent affinity for substrate (KS) implying the non-competitive nature of activation which indicated ...
... electrophoresis shows the decrease in electrophoretic
mobility of pepsin and confirms modification of the electric charge and conformational changes of pepsin caused by bound
Al on the pepsin molecule. AL induced conformational changes of pepsin were verified by UV-VIS and IR spectra.
Moreover, the absence ...
...
shown that Al'* ions inhibited trypsin activity, but do
not pepsin. It was observed highest activation of
pepsin activity by 191% in the presence of 25 ag AP?/
mL of reaction mixture [25].
As the mechanism of Al'* ions on pepsin activity is
not still clear, the objective of this study is to ...
... [AU](M)
Figure 1. Relative activity of pepsin in the presence of AP * ions.
Proteolytic activity of pepsin expressed as percentage depends on
A ions present. The degree of activation is expressed as % of
increased activity considering the activity of pepsin in the absence of
Al ions as 100%. All ...
Vesna M. Pavelkić, Kristina R. Gopcević, Danijela Z. Krstić, Marija A. Ilić. "The influence of Al3+ion on porcine pepsin activityin vitro" in Journal of Enzyme Inhibition and Medicinal Chemistry, Informa UK Limited (2008). https://doi.org/10.1080/14756360701841095
