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Histochemical Demonstration of a Species-Specific Trypsin-like Enzyme in Mast Cells

Abstract

DURING the investigation of a new histochemical substrate, Nα-benzoyl-dl-arginine-β-naphthylamide liydrochloride, localization by a simultaneous azo coupling reaction of enzymatic activity to mast cells in human and dog tissues was noted. Recently, Benditt has described the presence of an enzyme in the mast cells of numerous species resembling bovine α-chymotrypsin. This enzyme hydrolyses the histochemical substrate 3-chloroacetyl-2-naphthoic acid anilide1. Although Nα-benzoyl-dl-arginine-β-naphthylamide hydrochloride has been shown in biochemical systems to be a substrate for trypsin and not for α-chymotrypsin, carboxypeptidase, liver esterase or ‘leucine’ aminopeptidase2, it was thought of importance to attempt to define as closely as possible the characteristics of the enzyme in mast cells hydrolysing Nαa - benzoyl - dl - arginine - β - naphthylamide hydrochloride and to differentiate it from other known mast cell enzymes.

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References

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GLENNER, G., COHEN, L. Histochemical Demonstration of a Species-Specific Trypsin-like Enzyme in Mast Cells. Nature 185, 846–847 (1960). https://doi.org/10.1038/185846a0

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