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The Journal of Immunology, 1976, 117: 1039-1044.
Copyright © 1976 by The American Association of Immunologists, Inc.
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Separation of Slow Reacting Substance of Anaphylaxis (SRS-A) from Human Lung Into Four Biologically Active Fractions

Hidenobu Takahashi1, Marion E. Webster2 and Harold H. Newball

Laboratory of Chemistry, National Heart and Lung Institute, Bethesda, Maryland 20014, and the Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

Abstract

Slow reacting substance of anaphylaxis (SRS-A) was released from human lung passively sensitized with ragweed antibody and challenged with specific antigen E. After purification by ethanol extraction, incubation with alkali (0.1 M NaOH for 30 min at 37°C) and chromatography on silicic acid and DEAE-cellulose, human SRS-A was separated into four biologically active fractions (Fractions I to IV). Arylsulfatase (Type H-1) in 0.1 M sodium acetate buffer, pH 4.5, destroyed the biologic activity of only Fraction I. All four fractions, like SO4-, inhibited the arylsulfatase activity at pH 4.5 but not at pH 6.0 when p-nitrocatechol sulfate was used as substrate. These results suggest that SRS-A contain a sulfur group and that human SRS-A, like the prostaglandins, may be a family of compounds. The instability of the purified SRS-A to storage remains a major barrier to their further purification and chemical identification.

Footnotes

1 Present address: Department of Hygienic Chemistry, Meiji College of Pharmacy, 35-23 Nozawa-1, Setagaya-ku. Tokyo 154, Japan.

2 Please address correspondence to: Dr. Marion E. Webster, Building 10, Room 7N 323, National Heart and Lung Institute, Bethesda, MD 20014.






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