Dec 1, 1976

Functional characterization of rat mast cell arylsulfatase activity

The Journal of Immunology : Official Journal of the American Association of Immunologists
R P Orange, E G Moore

Abstract

Extracts of isolated rat peritoneal mast cells were demonstrated to contain appreciable quantities of arysulfatase 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 of 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.

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Mentioned in this Paper

Eosinophil
Sephadex G 200
Lung
Mast Cell
Mucopolysaccharidosis VI
Chromatography, DEAE-Cellulose
Phosphate Measurement
Gel Chromatography
Arylsulfatase Activity
Lung Diseases

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Anaphylaxis

Anaphylaxis is a serious allergic reaction that is rapid in onset and may cause death.

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