PMID: 40872Aug 1, 1979

Human platelet arylsulphatases: identification and capacity to destroy SRS-A

Immunology
D D MetcalfeM Kaliner

Abstract

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.

Related Concepts

Sulfates, Inorganic
Gamma-Thrombin
Pseudo Arylsulfatase A
Orthophosphate
SRS-A
Hydrogen-Ion Concentration
Blood Platelets
Sulfatases

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