Reconstitution of Escherichia coli thioredoxin from complementing peptide fragments obtained by cleavage at methionine-37 or arginine-73.
Open Access
- 1 February 1975
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 250 (4) , 1340-1347
- https://doi.org/10.1016/s0021-9258(19)41819-x
Abstract
No abstract availableKeywords
This publication has 29 references indexed in Scilit:
- Principles that Govern the Folding of Protein ChainsScience, 1973
- Inactivation of staphylococcal nuclease by the binding of antibodies to a distinct antigenic determinantBiochemistry, 1972
- Thioredoxin‐C′: Reconstitution of an active form of Escherichia coli thioredoxin from two noncovalently linked cyanogen bromide peptide fragmentsFEBS Letters, 1972
- Reversible Chemical Modification of the Tryptophan Residues of Thioredoxin from Escherichia coli BEuropean Journal of Biochemistry, 1972
- Immunochemistry of sperm whale of myoglobin. IX. Specific interaction of peptides obtained by cleavage at arginine peptide bondsBiochemistry, 1971
- Thioredoxin. 6. The Amino Acid Sequence of the Protein from Escherichia coli BEuropean Journal of Biochemistry, 1968
- Reversible acetoacetylation of amino groups in proteinsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1968
- Thioredoxin 2: Cleavage with Cyanogen BromideEuropean Journal of Biochemistry, 1967
- Separation of dansyl-amino acids by polyamide layer chromatographyBiochimica et Biophysica Acta (BBA) - Protein Structure, 1967
- Antigen — Antibody Reactions In GelsActa Pathologica Microbiologica Scandinavica, 1949