Application

A complex between plasmin and an inhibitor has been isolated in a study via affinity chromatography from urokinase-activated human plasma. It has also been used in a study to investigate activation of human epithelial sodium channel (ENaC) by plasmin and chymotrypsin.

Biochem/physiol Actions

Plasmin exhibits preferential cleavage at the carboxyl side of lysine and arginine residues with higher selectivity than trypsin. Converts polymerized fibrin into soluble products.pH Optimum: 8.5pH 7.5: ~40% of maximal activity, pH 9.5: ~50% of maximal activityTemperature Optimum: 37 °C with rapid inactivation at 56 °C

It is inhibited by α 2-antiplasmin and its interaction with fibrin is blocked. It digests the N-terminal region of the cytoplasmic protein αsynuclein preventing its uptake by surrounding cells.

General description

Plasmin functions as a key enzyme of the fibrinolytic cascade, and is also important in inflammation processes.

Packaging

Package size based on protein content

Physical form

Lyophilized powder containing sodium phosphate, mannitol, and NaCl.

Unit Definition

One unit will produce one μmole of p-Nitroanilide from D-Val-Leu-Lys-p-Nitroanilide per minute at pH 7.5 at 37 °C.