J Integr Plant Biol. ›› 1999, Vol. 41 ›› Issue (8): -.

• Research Articles •    

Biological Characterization of Heat-stable Antifreeze Proteins from Leaves of Ammopiptanthus mongolicus

WEI Ling-Bo, JIANG Yong, SHU Nian-Hong, GAO Su-Qin and FEI Yun-Biao   

Abstract: Antifreeze protein(afp) was purified from the heat stable proteins in the leaves of Ammopiptanthus mongolicus (Maxim.) Cheng f. by two-dimensional electrophoresis-electrophoretic elution. Its molecular weight and pi are about 40 kD and 9.0 respectively, and its thermal hysteresis activity (THA) is 0.9 ℃ at 20 g/L. afp is different from other antifreeze proteins. The N-terminal 20 amino acids of afp is SDDLSFTFNKFVPCQTDILF. alp is abundant in leaves and may play an important role in the antifreeze process in A. mongolicus during the period of ovenwintering.

Key words: Ammopiptanthus mongolicus, Heat stable proteins, Thermal hysteresis activity, Antifreeze protein (afp)

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