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(UMI)AAI9021748 http://hdl.handle.net/2142/20201 eng Daniel, William L. Ruoff, Berthie Marie 2011-05-07T12:32:04Z 2011-05-07T12:32:04Z 10000-01-01 1990 Arylsulfatases (arylsulfate sulfohydrolase, EC 3.1.6.1) catalyze the hydrolysis of the O-S bond of sulfate esters. Two types of arylsulfatases have been described based on their subcellular distribution and biochemical properties. Arylsulfatase C, a Type I enzyme, shares many properties with the steroid sulfatases: estrone-sulfate sulfatase (E1S-sulfatase) and dehydroepiandrosterone-sulfate sulfatase (DHEAS-sulfatase). They have similar subcellular localization, are membrane bound, have alkaline pH optima, are resistant to inhibition by sulfate and phosphate, and are glycoproteins. The goal of this thesis was to determine the relationship of arylsulfatase C to the steroid sulfatases in mammalian liver. Arylsulfatase C, DHEAS-sulfatase, and E1S-sulfatase activities were monitored during purification of the enzyme from liver of selected mammals. The enzymes were characterized by biochemical and immunological parameters. In the liver of rat, dog, cow, baboon, cat, and pig, arylsulfatase C and steroid sulfatase (arylsulfatase and alkylsulfatase) appear to be the same enzyme. In squirrel and guinea-pig liver, arylsulfatase (arylsulfatase C and E1S-sulfatase) and alkylsulfatase (DHEAS-sulfatases) activities are distinct. Pig liver also contains a distinct DHEAS-sulfatase, in addition to a single enzyme which has both arylsulfatase and alkylsulfatase activities. In sheep, goat, and human liver it is possible that all three activities are distinct, indicating that arylsulfatase C may hydrolyze another as yet unknown natural substrate distinct from steroid sulfates. Made available in DSpace on 2011-05-07T12:32:04Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9021748.pdf: 3617403 bytes, checksum: 3e4cc60bfe3438637f46dca54ce68ec3 (MD5) Previous issue date: 1990 Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T14:42:18Z Item is restricted indefinitely. Restriction data tranferred 2014-07-01T11:18:22-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission ETDs are only available to UIUC Users without author permission U of I Only AAI9021748 Copyright 1990 Ruoff, Berthie Marie Biology, General Chemistry, Biochemistry The relationship of arylsulfatase C and the steroid sulfatases in mammals text Biology Biology University of Illinois at Urbana-Champaign Dissertation Ph.D.