Refolding of bovine serum albumin and its proteolytic fragments. Regain of disulfide bonds, secondary structure, and ligand-binding ability.
Open Access
- 4 January 1981
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 256 (1) , 445-450
- https://doi.org/10.1016/s0021-9258(19)70157-4
Abstract
No abstract availableThis publication has 34 references indexed in Scilit:
- The folding of pancreatic elastase: Independent domain refolding and inter-domain interactionBiochemical and Biophysical Research Communications, 1978
- Conformational restrictions on the pathway of folding and unfolding of the pancreatic trypsin inhibitorJournal of Molecular Biology, 1977
- Bovine serum albumin as a catalyst. 5. A sensitive assay of the correct refolding of individual fragments of the proteinJournal of the American Chemical Society, 1976
- Fragments of bovine serum albumin produced by limited proteolysis. Conformation and ligand bindingBiochemistry, 1975
- Purification and properties of fragments of bovine serum albumin. I. Fragments of bovine serum albumin produced by limited proteolysis. Isolation and characterization of tryptic fragmentsBiochemistry, 1975
- Pathways of folding of reduced bovine pancreatic ribonucleaseBiochemistry, 1974
- CONFORMATIONAL STUDIES ON LARGE FRAGMENTS OF BOVINE SERUM ALBUMIN IN RELATION TO THE STRUCTURE OF THE MOLECULEInternational Journal of Peptide and Protein Research, 1974
- Sulfhydryl-catalyzed isomerization of bovine mercaptalbuminBiochemistry, 1973
- Nucleation, Rapid Folding, and Globular Intrachain Regions in ProteinsProceedings of the National Academy of Sciences, 1973
- Reversible sulfhydryl-catalyzed structural alteration of bovine mercaptalbuminBiochemistry, 1971