Purification of boiling-soluble antifreeze protein from the legume Ammopiptanthus mongolicus.
A boiling-soluble antifreeze protein (AFP) was purified from the winter leaves of Ammopiptanthus mongolicus an evergreen legume species surviving in the cold desert of northwest of China. Purification was achieved by using a procedure consisting of a heat treatment step followed by consecutive chromatography, including ion-exchange chromatography (DEAE-Cellulose 52, Source 15Q), molecular exclusion chromatography with Sephacryl S300, and hydrophobic interaction chromatography (Poros 20HP2). This AFP showed thermal hysteresis activity and could modify the normal growth of ice crystals. The thermal hysteresis activity (THA) of this purified antifreeze protein is 0.15 degrees C at a concentration of 10 mg/mL, and its molecular mass is approximately 28 kD by SDS-PAGE analysis.
Wang
Weixiang
W
College of Chemistry Technology, Dalian University of Technology, Dalian, P.R. China wangweixiang2001@yahoo.com.cn
Wei
Lingbo
L
D021301:Antifreeze Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification*; D002845:Chromatography / Q000379:methods*; D003460:Crystallization; D007887:Fabaceae / Q000737:chemistry* / Q000145:classification / Q000378:metabolism; D006358:Hot Temperature; D007053:Ice; D018515:Plant Leaves / Q000737:chemistry* / Q000145:classification / Q000378:metabolism; D012621:Seasons; D014867:Water / Q000737:chemistry*
D021301:Antifreeze Proteins; D007053:Ice; D014867:Water