The physico-chemical characterization of a boiling stable antifreeze protein from a perennial grass (Lolium perenne).
We have characterized a cold-induced, boiling stable antifreeze protein. This highly active ice recrystallization inhibition protein shows a much lower thermal hysteresis effect and displays binding behavior that is uncharacteristic of any AFP from fish or insects. Ice-binding studies show it binds to the (1 0 1 0) plane of ice and FTIR studies reveal that it has an unusual type of highly beta-sheeted secondary structure. Ice-binding studies of both glycosylated and nonglycosylated expressed forms indicate that it adsorbs to ice through the protein backbone. These results are discussed in light of the currently proposed mechanisms of AFP action.
Pudney
P D A
PD
Unilever Research, Colworth House, Sharnbrook, Bedford MK44 1LQ, UK. Paul.Pudney@unilever.com
Buckley
S L
SL
Sidebottom
C M
CM
Twigg
S N
SN
Sevilla
M-P
MP
Holt
C B
CB
Roper
David
D
Telford
J H
JH
McArthur
A J
AJ
Lillford
P J
PJ
D000818:Animals; D021301:Antifreeze Proteins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism; D005399:Fishes; D006358:Hot Temperature; D007053:Ice; D008129:Lolium / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature
D021301:Antifreeze Proteins; D007053:Ice; D010455:Peptides