Separation of slow reacting substance of anaphylaxis (SRS-A) from human lung into four biologically active fractions.
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 degrees 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 STS-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.
D001192:Arylsulfatases / Q000037:antagonists & inhibitors; D002845:Chromatography; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008168:Lung / Q000276:immunology*; D011830:Radiation Effects; D013189:SRS-A / Q000032:analysis* / Q000494:pharmacology / Q000528:radiation effects; D014466:Ultraviolet Rays
D013189:SRS-A; D001192:Arylsulfatases