Abstract
Barley LTP1 belongs to a large family of plant proteins termed non-specific lipid transfer proteins. The in vivo function of these proteins is unknown, but it has been suggested that they are involved in responses towards stresses such as pathogens, drought, heat, cold and salt. Also, the proteins have been suggested as transporters of monomers for cutin synthesis. We have analysed the stability of LTP1 towards denaturant, heat and proteases and found it to be a highly stable protein, which apparently does not denature at temperatures up to 100 degrees C. This high stability may be important for the biological function of LTP1.
| Original language | English |
|---|---|
| Journal | F E B S Letters |
| Volume | 488 |
| Issue number | 3 |
| Pages (from-to) | 145-8 |
| Number of pages | 4 |
| ISSN | 0014-5793 |
| Publication status | Published - 2001 |
Keywords
- Antigens, Plant
- Calorimetry, Differential Scanning
- Carrier Proteins
- Endopeptidases
- Guanidine
- Hordeum
- Hot Temperature
- Hydrogen-Ion Concentration
- Pepsin A
- Plant Proteins
- Protein Conformation
- Protein Denaturation
- Protein Folding
- Thermodynamics
- Thermolysin