Surprisingly high stability of barley lipid transfer protein, LTP1, towards denaturant, heat and proteases.
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.
Lindorff-Larsen
K
K
Carlsberg Laboratory, Department of Yeast Genetics, Gamle Carlsberg Vej 10, DK-2500, Copenhagen Valby, Denmark.
Winther
J R
JR
D052179:Antigens, Plant; D002152:Calorimetry, Differential Scanning; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism*; D010450:Endopeptidases / Q000378:metabolism*; D019791:Guanidine / Q000494:pharmacology; D001467:Hordeum / Q000737:chemistry*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D010434:Pepsin A / Q000378:metabolism; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation / Q000187:drug effects; D011489:Protein Denaturation / Q000187:drug effects; D017510:Protein Folding; D013816:Thermodynamics; D013820:Thermolysin / Q000378:metabolism
D052179:Antigens, Plant; D002352:Carrier Proteins; D010940:Plant Proteins; C511920:lipid transfer proteins, plant; D010450:Endopeptidases; D010434:Pepsin A; D013820:Thermolysin; D019791:Guanidine