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Thompson, D. Bruce 2015-05-14T15:21:27Z 2015-05-14T15:21:27Z 10000-01-01 1987 1987 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. http://hdl.handle.net/2142/77686 (UMI)AAI8803221 eng Biology, General Chemistry, Biochemistry The Comparative Biochemistry of Mammalian Arylsulfatases a and B text Chemistry and Chemical Engineering Biochemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.