| Literature DB >> 40872 |
D D Metcalfe, L M Corash, M 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.Entities:
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Year: 1979 PMID: 40872 PMCID: PMC1457150
Source DB: PubMed Journal: Immunology ISSN: 0019-2805 Impact factor: 7.397