{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/20201"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/20201","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"The relationship of arylsulfatase C and the steroid sulfatases in mammals","abstract":"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.","abstract_html":"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.","abstract_has_math":false,"creators":["Ruoff, Berthie Marie"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biology","degree_department":null,"school":null,"contributors":["Daniel, William L."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011-05-07T12:32:04Z","date_published":"2011-05-07T12:32:04Z","updated_at":"2026-07-22T22:25:15Z","subjects":["Biology, General","Chemistry, Biochemistry"],"languages":["eng"],"rights":["Copyright 1990 Ruoff, Berthie Marie"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(UMI)AAI9021748","AAI9021748"],"render_values":[{"text":"(UMI)AAI9021748","href":null,"code":true},{"text":"AAI9021748","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/20201","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Daniel, William L."]},{"key":"dc:creator","label":"Author","values":["Ruoff, Berthie Marie"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2011-05-07T12:32:04Z","10000-01-01","1990"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biology, General","Chemistry, Biochemistry"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 1990 Ruoff, Berthie Marie"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["(UMI)AAI9021748","http://hdl.handle.net/2142/20201","AAI9021748"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["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"]},{"key":"dc:title","label":"Title","values":["The relationship of arylsulfatase C and the steroid sulfatases in mammals"]}]}],"canonical_facts":{"dc:contributor":["Daniel, William L."],"dc:creator":["Ruoff, Berthie Marie"],"dc:date":["2011-05-07T12:32:04Z","10000-01-01","1990"],"dc:description":["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"],"dc:identifier":["(UMI)AAI9021748","http://hdl.handle.net/2142/20201","AAI9021748"],"dc:language":["eng"],"dc:rights":["Copyright 1990 Ruoff, Berthie Marie"],"dc:subject":["Biology, General","Chemistry, Biochemistry"],"dc:title":["The relationship of arylsulfatase C and the steroid sulfatases in mammals"],"dc:type":["text"],"thesis:degree_discipline":["Biology"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:25:15Z"}