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Functional Characterization of Rat Mast Cell Arylsulfatase Activity¹

From the Department of Immunology, Research Institute of the Hospital For Sick Children at the University of Toronto, Toronto, Ontario, Canada, M5G 1X8

Abstract

Extracts of isolated rat peritoneal mast cells were demonstrated to contain appreciable quantities of arylsulfatase activity. The enzyme was inhibited by both phosphate and sulfate ions and demonstrated a pH optimum of 5.0. The enzyme was recovered in the eluate of DE-52 columns and appeared to have a m.w. of 150,000 on Sephadex G-200 gel filtration. These findings and the anomalous kinetic behavior of the enzyme suggest that at least part of the enzymatic activity is of the arylsulfatase IIA type. While spontaneous release of the enzyme was observed, challenge of isolated rat mast cells with a goat anti-rat IgE serum resulted in a significant increase in release of the enzyme. The arylsulfatase activity extracted from isolated rat mast cells demonstrated comparable activity in inactivating slow reacting substance of anaphylaxis (SRS-A) to that described for human eosinophil and lung arylsulfatase.

Footnotes

¹ This work was supported by Grant MT-4605 from the Medical Research Council of Canada.