Isolation and characterization of sheep pepsin

Area of Science:

• Biochemistry
• Enzymology

Background:

• Pepsin is a key digestive enzyme.
• Understanding pepsin from different species aids in comparative enzymology.

Purpose of the Study:

• To isolate and characterize sheep pepsin.
• To compare sheep pepsin's properties with other mammalian pepsins.

Main Methods:

• Purification using pH fractionation, Sepharose 4B-poly-L-lysine chromatography, and Sephadex G-100 gel filtration.
• Enzyme kinetics and amino acid composition analysis.

Main Results:

• Sheep pepsin purified approx. 120-fold with a molecular weight of 34,000 Da.
• Similar amino acid composition to pig and ox pepsins, with a low basic residue content.
• Optimal activity at pH 1.8 for NN-dimethyl-casein and NN-dimethyl-haemoglobin, with kinetic parameters comparable to other pepsins.

Conclusions:

• Sheep pepsin exhibits biochemical properties similar to other mammalian pepsins.
• The enzyme's characteristics suggest its utility in biochemical research and comparative studies.