Purification and structure analysis of antifreeze proteins from Ammopiptanthus mongolicus.
We purified many kinds of antifreeze proteins with high activity from the leaves of Ammopiptanthus mongolicus by several biochemical techniques. The antifreeze activities of these AFPs were measured by both osmometry and differential scanning calorimetry, and the inhibition of growth of ice crystals by the AFPs was obvious. Additionally, the antifreeze proteins were analyzed by sequencing, glycosylation reaction, mass spectroscopy, and circular dichroism spectroscopy. Both samples have some other unique structures different from those of fishes and of insects. It was suggested that plant AFPs might have a particular antifreeze mechanism in comparison with that of fish and insects.
Fei
Y B
YB
Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, PR China.
Cao
P X
PX
Gao
S Q
SQ
Wang
B
B
Wei
L B
LB
Zhao
J
J
Chen
G
G
Wang
B H
BH
D000595:Amino Acid Sequence; D021301:Antifreeze Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D007887:Fabaceae / Q000378:metabolism*; D008969:Molecular Sequence Data; D011487:Protein Conformation
D021301:Antifreeze Proteins