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Purification and Some Properties of a Daucus carota Lectin which Enhances the Activation of Prophenoloxidase by CaCl2
Author(s) -
Irene Söderhäll,
Annika Bergenstråhle,
Kenneth Söderhäll
Publication year - 1990
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.93.2.657
Subject(s) - daucus carota , prophenoloxidase , lectin , biochemistry , biology , botany , receptor , innate immune system
Carrot (Daucus carota) cell cultures were found to secrete a protein, with the molecular weight of 58,000, which could strongly enhance the activation of carrot prophenoloxidase by CaCl(2). The protein was isolated from the culture filtrate and purified to electrophoretic homogeneity. The purified protein did also show hemagglutinating activity toward rat as well as rabbit erythrocytes and this activity was inhibitied by N-acetylglucosamine or fetuin.

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