NMR-STUDIES OF A MURINE-HUMAN CHIMERA OF LEUKEMIA INHIBITORY FACTOR (LIF) - COMPARISON WITH HUMAN LIF
- Author(s)
- Maurer, T; Smith, DK; Owczarek, CM; Layton, MJ; Zhang, JG; Nicola, NA; Norton, RS;
- Details
- Publication Year 1994,Volume 11,Issue #4,Page 271-276
- Journal Title
- GROWTH FACTORS
- Publication Type
- Journal Article
- Abstract
- Leukaemia inhibitory factor (LIF) is a polyfunctional cytokine active on many cell types. We present here H-1 NMR studies on the solution properties and stability of MH35, a chimera of murine and human LIF which can be expressed at high levels in Escherichia coli, thus enabling efficient labelling of the protein with the stable isotopes C-13 and N-15. MH35 has 85% sequence identity with human LIF and similar activity in biological assays. The H-1 chemical shifts of the 12 conserved aromatic residues and the pK(a) values of the five conserved histidine residues in MH35 and human LIF are very similar. Temperature dependence studies indicate that both proteins are stable, with significant conformational changes occurring only above 70 degrees C. These results show that these proteins have a similar overall structure and stability and that MH35 is therefore a suitable analogue of human LIF for structural studies in solution.
- Publisher
- HARWOOD ACAD PUBL GMBH
- Keywords
- COLONY-STIMULATING FACTOR; SPECTROSCOPY
- Publisher's Version
- https://doi.org/10.3109/08977199409010999
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 1994-01-01 12:00:00