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Non-pancreatic Proteases Of The Chymotrypsin Family. I. A Chymotrypsin-like Protease From Rat Mast Cells.

J. Kawiak, W. Vensel, J. Komender, E. Barnard
Published 1971 · Chemistry, Medicine

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Abstract A protease has been purified from the isolated granules of mast cells from the peritoneal cavity of the rat. It resembles pancreatic chymotrypsin in most functional aspects, and has (by gel filtration measurement) the same molecular weight. It is active on tyrosine esters, but not arginine esters, and has a pH optimum and Michaelis constant in the hydrolysis of benzoyl- l -tyrosine ethyl ester (BTEE) that are very similar to those for bovine α-chymotrypsin. It exhibits the active-center-directed reactivities that are associated with the serine and with the histidine residues in chymotrypsin. There is evidence to suggest that it exists in the mast cell not as a zymogen, but as the active enzyme, bound to heparin. This enzyme exhibits an exceptional affinity for Sephadex or Bio-Gel gels, and is strongly retarded in filtration on these in neutral 0.1 M salt solutions. This leads to large errors in molecular weight estimation, which are removed when the filtration is conducted in 1.4 M KCl solution. The origin of such anomalies on the gel columns is discussed.
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