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Isolation and characterization of rat hepatic ascorbic acid-2-sulfatases
Enzyme
|January 1, 1987
Summary
Researchers isolated and purified rat liver ascorbic acid-2-sulfatase, identifying arylsulfatase A and B as key enzymes responsible for its cationic and anionic forms, respectively.
Area of Science:
- Biochemistry
- Enzymology
Background:
- Ascorbic acid-2-sulfatase is an enzyme crucial for ascorbic acid metabolism.
- Understanding its enzymatic properties and isoforms is important for biochemical research.
Purpose of the Study:
- To isolate and characterize ascorbic acid-2-sulfatase from rat liver.
- To identify the specific arylsulfatases responsible for its different activities.
Main Methods:
- Multistep purification procedure.
- DEAE Sephacel ion-exchange chromatography.
- Enzyme activity assays comparing hydrolysis rates.
Main Results:
- Ascorbic acid-2-sulfatase was resolved into cationic and anionic fractions with 75- and 230-fold purification.
- Arylsulfatase B was linked to cationic activity, and arylsulfatase A to anionic activity.
- Partially purified arylsulfatase A showed 4% and arylsulfatase B showed 0.6% the rate of p-nitrocatechol sulfate hydrolysis for ascorbic acid-2-sulfate.
Conclusions:
- Rat liver contains distinct cationic and anionic forms of ascorbic acid-2-sulfatase.
- Arylsulfatase A and B are identified as the enzymes responsible for these activities.
- Differential substrate hydrolysis rates suggest distinct roles for these arylsulfatases.