Chymase human

Chymase is a cathepsin G-like, S1 serine proteinase found primarily in mast cells. It has a molecular mass of ~30 kDa, however its apparent molecular mass on SDS-PAGE is around 37 kDa.

Chymase has been implicated in generation of angiotensin II and cleavage of big endothelin. Studies indicate it may be involved in vascular proliferation, myocardial infarction and dermatitis.

Human chymase has been used in a study to assess the effects of Panax notoginseng flower extract on the TGF-β/Smad signal transduction pathway in heart remodeling. Human chymase has also been used in a study to investigate the blood glucose level and survival in streptozotocin-treated human chymase transgenic mice.

The enzyme rapidly converts angiotensin I to angiotensin II. Optimum pH for the enzyme activity is between 7.5 and 9.0. Enzyme activity is inhibited by soybean trypsin inhibitor, phenylmethylsulfonyl fluoride and chymostatin.

Supplied as a solution in 20 mM Tris, 0.8 M NaCl and 25% glycerol, pH 7.6

One unit hydrolyzes one micromole of N-benzoyl-L-tyrosine ethyl ester (BTEE) per minute at pH 7.8 and 25 °C. The assay buffer used to determine the enzyme activity contains 27 mM Tris-HCl, pH 7.8, with 150 mM NaCl and 0.43 mM BTEE.