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

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Surprisingly high stability of barley lipid transfer protein, LTP1, towards denaturant, heat and proteases. / Lindorff-Larsen, Kresten; Winther, Jakob R.

I: FEBS Letters, Bind 488, Nr. 3, 2001, s. 145-148.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Lindorff-Larsen, K & Winther, JR 2001, 'Surprisingly high stability of barley lipid transfer protein, LTP1, towards denaturant, heat and proteases', FEBS Letters, bind 488, nr. 3, s. 145-148.

APA

Lindorff-Larsen, K., & Winther, J. R. (2001). Surprisingly high stability of barley lipid transfer protein, LTP1, towards denaturant, heat and proteases. FEBS Letters, 488(3), 145-148.

Vancouver

Lindorff-Larsen K, Winther JR. Surprisingly high stability of barley lipid transfer protein, LTP1, towards denaturant, heat and proteases. FEBS Letters. 2001;488(3):145-148.

Author

Lindorff-Larsen, Kresten ; Winther, Jakob R. / Surprisingly high stability of barley lipid transfer protein, LTP1, towards denaturant, heat and proteases. I: FEBS Letters. 2001 ; Bind 488, Nr. 3. s. 145-148.

Bibtex

@article{64a2a89c5a2c471ebd26b45b476f9b5e,
title = "Surprisingly high stability of barley lipid transfer protein, LTP1, towards denaturant, heat and proteases",
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.",
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",
author = "Kresten Lindorff-Larsen and Winther, {Jakob R.}",
year = "2001",
language = "English",
volume = "488",
pages = "145--148",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "3",

}

RIS

TY - JOUR

T1 - Surprisingly high stability of barley lipid transfer protein, LTP1, towards denaturant, heat and proteases

AU - Lindorff-Larsen, Kresten

AU - Winther, Jakob R.

PY - 2001

Y1 - 2001

N2 - 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.

AB - 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.

KW - Antigens, Plant

KW - Calorimetry, Differential Scanning

KW - Carrier Proteins

KW - Endopeptidases

KW - Guanidine

KW - Hordeum

KW - Hot Temperature

KW - Hydrogen-Ion Concentration

KW - Pepsin A

KW - Plant Proteins

KW - Protein Conformation

KW - Protein Denaturation

KW - Protein Folding

KW - Thermodynamics

KW - Thermolysin

M3 - Journal article

C2 - 11163761

VL - 488

SP - 145

EP - 148

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 3

ER -

ID: 37849216