Purification and characterization of recombinant hydroxysteroid sulfotransferase

Authors

  • Michael J. Huey Laboratory for Cellular and Biochemical Toxicology, College of Pharmacy Rutgers University, Piscataway, NJ
  • Frederick C. Kauffman Laboratory for Cellular and Biochemical Toxicology, College of Pharmacy Rutgers University, Piscataway, NJ

Abstract

Sulfotransferases are important enzymes involved in the conjugation of many foreign chemicals and endogenous substances. The goal of work outlined in this paper was to heterologously express five different forms of this family of enzymes cloned from human and rat liver in bacteria. A second goal was to develop methods for the purification of these enzymes from bacterial cytosol. Expression of several forms of these enzymes was complicated by their deposition in bacterial inclusion bodies. Rules governing the deposition of sulfotransferases in inclusion bodies could not be developed on the basis of their secondary structures or enzymatic activities.

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Author Biography

Michael J. Huey, Laboratory for Cellular and Biochemical Toxicology, College of Pharmacy Rutgers University, Piscataway, NJ

Rutgers Undergraduate Research Fellow

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Published

1999-09-01

How to Cite

Huey, M. J. ., & Kauffman, F. C. . (1999). Purification and characterization of recombinant hydroxysteroid sulfotransferase. The Rutger Scholar, 1. Retrieved from https://rutgersscholar.libraries.rutgers.edu/index.php/scholar/article/view/6

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