Different conformation of purified human recombinant interleukin 1β from Escherichia coli and Saccharomyces cerevisiae is related to different level of biological activity
- 1 July 1989
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 162 (1) , 357-363
- https://doi.org/10.1016/0006-291x(89)92004-4
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- Mapping of a Protective Epitope of Pertussis Toxin by In Vitro Refolding of Recombinant FragmentsNature Biotechnology, 1988
- Muteins of human interleukin‐1 that show enhanced bioactivitiesFEBS Letters, 1987
- Purification and characterization of human recombinant interleukin-1 beta.Journal of Biological Chemistry, 1987
- A novel leader peptide which allows efficient secretion of a fragment of human interleukin 1 beta in Saccharomyces cerevisiae.The EMBO Journal, 1987
- Purification and characterization of human interleukin‐1β expressed in recombinant Escherichia coliEuropean Journal of Biochemistry, 1986
- Amino acid sequence analysis of human interleukin 1 (IL-1). Evidence for biochemically distinct forms of IL-1.The Journal of Experimental Medicine, 1985
- Cloning, sequence and expression of two distinct human interleukin-1 complementary DNAsNature, 1985
- Interleukin-1Clinical Infectious Diseases, 1984
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Tissue sulfhydryl groupsArchives of Biochemistry and Biophysics, 1959