Investigation of the Solubility and Enzymatic Activity of a Thioredoxin-Gelonin Fusion Protein
Abstract
A synthetic gene for the ribosome-inactivating protein (RIP), gelonin, was previously engineered and inserted into the pET-21a plasmid under the control of the T7 promoter by researchers at M.D. Anderson Cancer Research Institute in Houston, Texas. Upon induction of Escherichia coli (E. coli) strain BL-21(DE3)pLysS containing this pET-2 1 a/gel plasmid, the resulting gelonin protein forms insoluble aggregates, known as inclusion bodies, and exhibits no activity under the assay conditions tested. By genetically fusing gelonin to the highly stable and soluble protein, thioredoxin, it was thought that there would be an increase in the solubility of gelonin, possibly accompanied by a measurable amount of enzymatic activity.
Document Details
- Document Type
- Technical Report
- Publication Date
- May 01, 1997
- Accession Number
- ADA325566
Entities
People
- Michael J. Licata
Organizations
- University of Texas at Austin