α-Chymotrypsin from bovine pancreas

Appearance (description):lyophilisate
Appearance (colour):slightly yellowish
Activity (ATEE, pH 8.0, 25 °C):≥ 350 U/mg
Spec. activity (calc. on protein):ca. 400

α-Chymotrypsin has been used to study its adsorption characteristics on solid/liquid interfaces under varying adsorption conditions.

α-Chymotrypsin (CT) closely denotes a group of digestive enzymes (trypsin, elastase) that hydrolyzes polypeptide chains. The catalytic triad system works together to regulate the nucleophilicity of the serine residue in catalysis. CT shows a capability to catalyze nonconventional synthetic reactions in water-miscible organic media. Additionally, it is also used as a tool in comparative studies of water-miscible and water-immiscible solvents.

α-Chymotrypsin (CT) is a member of the S1 family. It comprises a catalytic triad system including aspartate, histidine, and serine. It is produced by chymotrypsinogen in the pancreas and then secreted into the digestive tract.