Human platelet arylsulphatases: identification and capacity to destroy SRS-A.
Arylsulphatases IIA and IIB have been separately identified in human platelets by use of anion exchange chromatography and gel filtration. Arylsulphatase IIA had a molecular weight of 160,000 and a pH optimum of 4.5. Arylsulphatase IIB had a molecular weight of 60,000 and a pH optimum of 5.5. Both arylsulphatases IIA and IIB were inhibited by phosphate and sulphate ions characteristic of this enzyme class. Platelets, upon exposure to ionophore A-23187 or thrombin, discharged arylsulphatase coincident with beta-glcuronidase release. Partially purified platelet arylsulphatase IIB inactivated rat SRS-A.
D001192:Arylsulfatases / Q000037:antagonists & inhibitors / Q000097:blood*; D001792:Blood Platelets / Q000201:enzymology*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010710:Phosphates / Q000494:pharmacology; D013189:SRS-A / Q000037:antagonists & inhibitors*; D013429:Sulfatases / Q000097:blood*; D013431:Sulfates / Q000494:pharmacology; D013917:Thrombin
D010710:Phosphates; D013189:SRS-A; D013431:Sulfates; D013429:Sulfatases; D001192:Arylsulfatases; D013917:Thrombin