Yb. Fei et al., Isolation, purification and characterization of secondary structure of antifreeze protein from Ammopiptanthus mongolicus, CHIN SCI B, 46(6), 2001, pp. 495-498
Antifreeze protein(AFP) from Ammopiptanthus mongolicus leaves was isolated
and purified with DEAE cellulose 52, Sephacryl 300, heat treatment and prep
arative isotachophoresis. The molecular weight of AFP was 50 ku by SDS-PAGE
measurement. The average thermal hysteresis activity (THA) of AFP was 0.35
degreesC at 5 mg/mL using a differential scanning calorimeter (DSC). This
AFP showed heated stability. From circular dichroism (CD) of AFP spectral d
ata from 195-240 nm, a well-defined secondary structure of 11% alpha -helix
, 34% antiparallel beta -sheet and 55% random coil for the plant AFP was de
duced.