Description
General description
Pepsin is an aspartic endoproteinase isolated from pig gastric mucosa. It is mainly used for the unspecific hydrolysis of proteins and peptides in acidic media. It also provides a limited hydrolysis of native immunoglobulins to yield biologically active fragments.
Application
Pepsin has been used for the digestion of liver tissue obtained from rat.
Biochem/physiol Actions
Aspartic endopeptidase with relatively broad specificity. Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1′ positions.
Preparation Note
Working concentration: 0.05 to 0.5 mg/ml
Storage conditions (working solution): A pepsin solution is stable at 2 to 8 °C, at least for one week, at neutral pH and under germfree conditions. Frozen aliquots of the enzyme solution are expected to be more stable.
A stock solution in 10 mM HCl (5-10 mg/ml) should be stable for at least one week at 2 to 8 °C, too. Storage light protected, tightly closed.
A short (2 minutes) incubation at 40 °C has negligible effect on the activity of lyophilized pepsin or pepsin in solution.
Analysis Note
At 37 °C with hemoglobin as the substrate. One unit is the enzyme activity which liberates the amount of Tyr producing an increase in the absorbance of 0.001/minute at 280 nm.
Other Notes
For life science research only. Not for use in diagnostic procedures.