{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/77686"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/77686","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"The Comparative Biochemistry of Mammalian Arylsulfatases a and B","abstract":"Arylsulfatases A and B are lysosomal hydrolases in mammals and appear essential for a number of biological processes, including vitamin C metabolism, fertilization, turnover of nerve membrane components, and degradation of connective tissue substances.","abstract_html":"Arylsulfatases A and B are lysosomal hydrolases in mammals and appear essential for a number of biological processes, including vitamin C metabolism, fertilization, turnover of nerve membrane components, and degradation of connective tissue substances.","abstract_has_math":false,"creators":["Thompson, D. Bruce"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-05-14T15:21:27Z","date_published":"2015-05-14T15:21:27Z","updated_at":"2026-07-22T22:26:11Z","subjects":["Biology, General","Chemistry, Biochemistry"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(UMI)AAI8803221"],"render_values":[{"text":"(UMI)AAI8803221","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/77686","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Thompson, D. Bruce"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-05-14T15:21:27Z","10000-01-01","1987"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry"]},{"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"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/77686","(UMI)AAI8803221"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Arylsulfatases A and B are lysosomal hydrolases in mammals and appear essential for a number of biological processes, including vitamin C metabolism, fertilization, turnover of nerve membrane components, and degradation of connective tissue substances.","Arylsulfatase A and B were isolated from liver tissue of several different mammals (mouse, rat, cow, opossum, deer, dog, pig, sheep, whale, cat, seal, and vole) using the sequence DEAE-Sephacel and Concanavalin A-Sepharose. The enzymes were characterized by examining their ability to hydrolyze four substrates (para-nitrocatechol sulfate (pNCS), 4 methyl-umbelliferyl sulfate (4MUS), ascorbic acid-2-sulfate (AA2S), and paranitrophenyl sulfate (pNPS)). The pNCS, 4MUS, and AA2S-sulfatase activities were further characterized on the basis of pH optima, response to inhibitors, enzyme kinetics, thermostabilities, relative molecular weights, isoelectric points, and precipitation by polyclonal anti-mouse arylsulfatase B IgG and anti-Bovine arylsulfatase A IgG. Arylsulfatase A was defined as an anionic isozyme which was inhibited by silver ions, displayed non-linear pNCS-sulfatase kinetics, and crossreacted with the anti-bovine arylsulfatase A IgG. Arylsulfatase B was considered to be a cationic arylsulfatase, which was not inhibited by silver ions, exhibited linear pNCS-sulfatase kinetics, and crossreacted with anti-mouse arylsulfatase B IgG.","Arylsulfatase A appeared in a multimeric form in all the species examined and was generally anionic in nature, except in the deer, pig, seal, and whale where a cationic form of arylsulfatase A was detected. However, arylsulfatase B was observed in both monomeric and dimeric forms; and in both cationic and anionic forms. The proportion of the monomeric and dimeric forms of arylsulfatase B differed among species. The opossum lacked detectable arylsulfatase B. The dog, pig, seal, whale, mouse, rat, and cow all possessed an anionic form of arylsulfatase B that had molecular weights and ionic properties that were similar to arylsulfatase A. In addition, all three rodents possessed an anionic form of arylsulfatase B that was monomeric and appeared unrelated to arylsulfatase B. (Abstract shortened with permission of author.)","Made available in DSpace on 2015-05-14T15:21:27Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 8803221.PDF: 5206842 bytes, checksum: fc0b7aa076c62d0b3a3ba6b86f920b06 (MD5) Previous issue date: 1987","Embargo set by: Seth Robbins for item 78896 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","241 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1987."]},{"key":"dc:title","label":"Title","values":["The Comparative Biochemistry of Mammalian Arylsulfatases a and B"]}]}],"canonical_facts":{"dc:creator":["Thompson, D. Bruce"],"dc:date":["2015-05-14T15:21:27Z","10000-01-01","1987"],"dc:description":["Arylsulfatases A and B are lysosomal hydrolases in mammals and appear essential for a number of biological processes, including vitamin C metabolism, fertilization, turnover of nerve membrane components, and degradation of connective tissue substances.","Arylsulfatase A and B were isolated from liver tissue of several different mammals (mouse, rat, cow, opossum, deer, dog, pig, sheep, whale, cat, seal, and vole) using the sequence DEAE-Sephacel and Concanavalin A-Sepharose. The enzymes were characterized by examining their ability to hydrolyze four substrates (para-nitrocatechol sulfate (pNCS), 4 methyl-umbelliferyl sulfate (4MUS), ascorbic acid-2-sulfate (AA2S), and paranitrophenyl sulfate (pNPS)). The pNCS, 4MUS, and AA2S-sulfatase activities were further characterized on the basis of pH optima, response to inhibitors, enzyme kinetics, thermostabilities, relative molecular weights, isoelectric points, and precipitation by polyclonal anti-mouse arylsulfatase B IgG and anti-Bovine arylsulfatase A IgG. Arylsulfatase A was defined as an anionic isozyme which was inhibited by silver ions, displayed non-linear pNCS-sulfatase kinetics, and crossreacted with the anti-bovine arylsulfatase A IgG. Arylsulfatase B was considered to be a cationic arylsulfatase, which was not inhibited by silver ions, exhibited linear pNCS-sulfatase kinetics, and crossreacted with anti-mouse arylsulfatase B IgG.","Arylsulfatase A appeared in a multimeric form in all the species examined and was generally anionic in nature, except in the deer, pig, seal, and whale where a cationic form of arylsulfatase A was detected. However, arylsulfatase B was observed in both monomeric and dimeric forms; and in both cationic and anionic forms. The proportion of the monomeric and dimeric forms of arylsulfatase B differed among species. The opossum lacked detectable arylsulfatase B. The dog, pig, seal, whale, mouse, rat, and cow all possessed an anionic form of arylsulfatase B that had molecular weights and ionic properties that were similar to arylsulfatase A. In addition, all three rodents possessed an anionic form of arylsulfatase B that was monomeric and appeared unrelated to arylsulfatase B. (Abstract shortened with permission of author.)","Made available in DSpace on 2015-05-14T15:21:27Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 8803221.PDF: 5206842 bytes, checksum: fc0b7aa076c62d0b3a3ba6b86f920b06 (MD5) Previous issue date: 1987","Embargo set by: Seth Robbins for item 78896 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","241 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1987."],"dc:identifier":["http://hdl.handle.net/2142/77686","(UMI)AAI8803221"],"dc:language":["eng"],"dc:subject":["Biology, General","Chemistry, Biochemistry"],"dc:title":["The Comparative Biochemistry of Mammalian Arylsulfatases a and B"],"dc:type":["text"],"thesis:degree_discipline":["Biochemistry"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:26:11Z"}