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首页> 外文期刊>Chinese science bulletin >Isolation, purification and characterization of secondary structure of antifreeze protein from Ammopiptanthus mongo- licus.
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Isolation, purification and characterization of secondary structure of antifreeze protein from Ammopiptanthus mongo- licus.

机译：蒙古沙虫抗冻蛋白二级结构的分离，纯化和鉴定。

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摘要

Antifreeze protein (AFP) from Ammopiptanthus mongolicus leaves was isolated and purified with DEAE cel- lulose 52, Sephacryl 300, heat treatment and was 50 ku by isotachophoresis. The molecular weight of AFP was 50 ku by SDS-PACE measurement. The average thermal hysteresis Activity (THA) of AFP was 0.35 deg. C at 5 mg/mL using a dif- Ferential scanning calorimeter (DSC). This AFP showed Heated stability. From circular dichrosim (CD) of AFP spec- Tral data from 195-240 nm, a well-defined secondary Structure of 11/100 α-helic, 34/100 antiparallel β-sheet and 55/100 Random coil for the plant AFP was deduced.
机译：分离并用DEAE纤维素52，Sephacryl 300，热处理纯化了沙冬青叶的抗冻蛋白（AFP），并通过等速电泳将其定为50 ku。通过SDS-PACE测量，AFP的分子量为50ku。 AFP的平均热滞后活性（THA）为0.35度。使用差示扫描量热仪（DSC）以5 mg / mL的温度洗脱。该AFP显示出加热的稳定性。从195-240 nm的AFP光谱数据的圆二色性（CD）得出，植物AFP的11/100α-螺旋，34/100反平行β-折叠和55/100无规卷曲的定义明确的二级结构为推论。

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