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Inactivation of Slow Reacting Substance of Anaphylaxis (SRS-A) by Arylsulfatases¹

From the Department of Immunology, Research Institute of The Hospital for Sick Children at the University of Toronto, Toronto, Ontario, the Department of Pharmacology, University of Colorado Medical School, Denver, Colorado, and the Department of Medicine, Harvard Medical School at the Robert B. Brigham Hospital, Boston, Massachusetts

Abstract

Two different arylsulfatase preparations inactivated slow reacting substance of anaphylaxis (SRS-A) in a dose-related fashion. The loss of SRS-A activity could not be attributed to -glucuronidase activity in the arylsulfatase preparations or to nonspecific adsorption to proteins. The arylsulfatase and SRS-A inactivating activities shared similar pH requirements, kinetics, and elution properties on Sephadex G-200 gel filtration. With spark source mass spectrometry, analysis of highly purified preparations of SRS-A revealed an abundance of ³²S and ⁴⁰Ca in the active samples as compared to controls. These findings indicate that SRS-A may contain a sulfate ester group.

Footnotes

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

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