Structure and enzymic functions of thioredoxin refolded by complementation of two tryptic peptide fragments
- 11 December 1979
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 18 (25) , 5584-5591
- https://doi.org/10.1021/bi00592a010
Abstract
Note: In lieu of an abstract, this is the article's first page.Keywords
This publication has 7 references indexed in Scilit:
- Thioredoxin-C': mechanism of noncovalent complementation and reactions of the refolded complex and the active site containing fragment with thioredoxin reductaseBiochemistry, 1979
- Thiroedoxin from Escherichia coli. Radioimmunological and enzymatic determinations in wild type cells and mutants defective in phage T7 DNA replication.Journal of Biological Chemistry, 1978
- Genetic mapping of trxA, a gene affecting thioredoxin in Escherichia coli K12Molecular Genetics and Genomics, 1977
- Escherichia coli thioredoxin: a subunit of bacteriophage T7 DNA polymerase.Proceedings of the National Academy of Sciences, 1976
- Thioredoxin. A Localized Conformational Change Accompanying Reduction of the Protein to the Sulfhydryl Form*Biochemistry, 1967
- THIOREDOXIN REDUCTASE - CHARACTERIZATION OF A HOMOGENEOUS PREPARATION FROM ESCHERICHIA COLI B1967
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964