Arylsulfatase B of human lung. Isolation, characterization, and interaction with slow-reacting substance of anaphylaxis.
Arylsulfatase B was separated from arylsulfatase A in extracts of human lung tissue by anion exchange chromatography and further purified by gel filtration and cation exchange chromatography. Arylsulfatase B of human lung was similar to that enzyme in other tissues and species, exhibiting an apparent mol wt of approximately 60,000, a pH optimum for cleavage of 4-nitrocatechol sulfate (pNCS) of 5.5-6.0, and a sensitivity to inhibition by phosphate ions and especially pyrophosphate in the presence of NaCl. Human lung arylsulfatase B inactivated slow-reacting substance of anaphylaxix (SRS-A) in a linear time-dependent reaction in which the rate was determined by the enzyme-to-substrate ratio. Cleavage of pNCS by human lung arylsulfatase B was competitively suppressed by SRS-A. The finding that human lung tissue contains predominately arylsulfatase B discloses a potential regulatory mechanism for inactivation of SRS-A at or near the site of its generation.
D002803:Chondro-4-Sulfatase / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D002845:Chromatography; D002850:Chromatography, Gel; D004347:Drug Interactions; D004804:Eosinophils / Q000201:enzymology; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008168:Lung / Q000201:enzymology*; D013189:SRS-A / Q000037:antagonists & inhibitors* / Q000302:isolation & purification; D013429:Sulfatases / Q000378:metabolism*
D013189:SRS-A; D013429:Sulfatases; D002803:Chondro-4-Sulfatase