Human interleukin‐5 expressed in Escherichia coli: assignment of the disulfide bridges of the purified unglycosylated protein
- 20 May 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 283 (1) , 61-64
- https://doi.org/10.1016/0014-5793(91)80553-f
Abstract
Human interleukin‐5 is a homodimer: each subunit contains two cysteine residues that form two inter‐subunit disulfide bonds. The topology of the disulfides in recombinant human interleukin‐5 produced in Escherichia coli was studied by proteolytic digestion and peptide mapping. Disulfide linked peptides containing cysteine 42 linked to cysteine 84 were isolated. This indicated that cysteine 42 and 84 of one subunit were linked in an antiparallel manner to cysteines 84 and 42 of the other subunit.Keywords
This publication has 18 references indexed in Scilit:
- Expression of Human and Murine Interleukin-5 in Eukaryotic SystemsDNA, 1989
- Structure and refinement of the oxidized P21 form of uteroglobin at 1.64 Å resolutionJournal of Molecular Biology, 1989
- Refined structure of glutathione reductase at 1.54 Å resolutionJournal of Molecular Biology, 1987
- Cloning of cDNA for human T-cell replacing factor (interieukin-5) and comparison with the murine homologueNucleic Acids Research, 1986
- Cloning of complementary DNA encoding T-cell replacing factor and identity with B-cell growth factor IINature, 1986
- The biology of platelet-derived growth factorCell, 1986
- Complementary DNA sequences of ovarian follicular fluid inhibin show precursor structure and homology with transforming growth factor-βNature, 1985
- Disulfide bond formation in proteinsPublished by Elsevier ,1984
- Interchain disulfide bridges in ribonuclease BS-1Biochemical and Biophysical Research Communications, 1973
- [26] Treatment of trypsin with TPCKPublished by Elsevier ,1967