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|Title:||The relationship of arylsulfatase C and the steroid sulfatases in mammals|
|Author(s):||Ruoff, Berthie Marie|
|Doctoral Committee Chair(s):||Daniel, William L.|
|Department / Program:||Biology|
|Degree Granting Institution:||University of Illinois at Urbana-Champaign|
|Abstract:||Arylsulfatases (arylsulfate sulfohydrolase, EC 126.96.36.199) 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.
|Rights Information:||Copyright 1990 Ruoff, Berthie Marie|
|Date Available in IDEALS:||2011-05-07|
|Identifier in Online Catalog:||AAI9021748|