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Enterokinase (enteropeptidase): comparative aspects.

Trends in biochemical sciences (1989-03-01)
A Light, H Janska
ABSTRACT

The serine protease enterokinase is the physiological activator of trypsinogen and has a specificity for the sequence (Asp)4-Lys-Ile. The enzyme consists of two subunits linked by a disulfide bond. The heavy chain achors enterokinase in the intestinal brush border membrane and the light chain is the catalytic subunit, which has the same mechanism of action as trypsin and chymotrypsin. Many properties of enterokinase resemble blood-clotting enzymes, suggesting that enterokinase lies on the same phylogenetic branch as the blood-clotting proteins.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Enterokinase from porcine intestine, ≥0.5 units/mg solid
Sigma-Aldrich
Enterokinase from porcine intestine, lyophilized powder, ≥100 units/mg protein
Sigma-Aldrich
Enterokinase from bovine intestine, powder