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

被引：120

作者：

Lindorff-Larsen, K ^{[1
]}

Winther, JR ^{[1
]}

机构：

[1] Carlsberg Lab, Dept Yeast Genet, DK-2500 Copenhagen, Denmark

来源：

FEBS LETTERS | 2001年 / 488卷 / 03期

关键词：

non-specific lipid transfer protein; barley; protein stability; protease digestion;

D O I：

10.1016/S0014-5793(00)02424-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 degreesC, This high stability may be important for the biological function of LTP1, (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：145 / 148

页数：4

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