Surprisingly high stability of barley lipid transfer protein, LTP1, towards denaturant, heat and proteases

FEBS Letters

Winther, Jakob R¹  Lindorff-Larsen, Kresten¹ 

[1] Carlsberg Laboratory, Department of Yeast Genetics, Gamle Carlsberg Vej 10, DK-2500 Copenhagen Valby, Denmark

关键词: Non-specific lipid transfer protein;    Barley;    Protein stability;    Protease digestion;    DSC;    differential scanning calorimetry;    GuaHCl;    guanidine hydrochloride;    ns-LTP;    non-specific lipid transfer protein;   

DOI  :  10.1016/S0014-5793(00)02424-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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°C. This high stability may be important for the biological function of LTP1.

【 授权许可】

Unknown