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Expression, purification and functional properties of a soluble form of <em>Bradyrhizobium japonicum</em> TlpA, a thioredoxin-like protein.
- Source :
- European Journal of Biochemistry; 7/15/94, Vol. 223 Issue 2, p339-344, 6p
- Publication Year :
- 1994
-
Abstract
- The TlpA protein of Bradyrhizobium japonicum was previously identified genetically as a membrane-anchored, periplasmic thioredoxin-like protein. Here we describe the heterologous expression in Escherichia coli, subsequent purification and biochemical characterization of TlpA. A soluble form of TlpA, which lacks its N-terminal membrane anchor, was overexpressed in E. coli and purified by a two-step procedure. Pure TlpA was shown to be a monomer in solution and was active in reducing the disulfides of insulin and in reactivating reduced, denatured RnaseA. Evidence is presented that two non-active-site cysteine residues form an intramolecular disulfide bond, a feature that is not normally found in other prokaryotic thioredoxins. [ABSTRACT FROM AUTHOR]
- Subjects :
- PROTEINS
THIOREDOXIN
GENE expression
ESCHERICHIA coli
INSULIN
BIOCHEMISTRY
Subjects
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 223
- Issue :
- 2
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 12692738
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1994.tb18999.x