Isolation and characterization of a novel antifreeze protein from carrot (Daucus carota).
A modified assay for inhibition of ice recrystallization which allows unequivocal identification of activity in plant extracts is described. Using this assay a novel, cold-induced, 36 kDa antifreeze protein has been isolated from the tap root of cold-acclimated carrot (Daucus carota) plants. This protein inhibits the recrystallization of ice and exhibits thermal-hysteresis activity. The polypeptide behaves as monomer in solution and is N-glycosylated. The corresponding gene is unique in the carrot genome and induced by cold. The antifreeze protein appears to be localized within the apoplast.
Smallwood
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M
The Plant Laboratory, Department of Biology, University of York, PO Box 373, York YO1 5YW, U.K. mfs1@york.ac.uk
Worrall
D
D
Byass
L
L
Elias
L
L
Ashford
D
D
Doucet
C J
CJ
Holt
C
C
Telford
J
J
Lillford
P
P
Bowles
D J
DJ
D021301:Antifreeze Proteins; D001483:Base Sequence; D015153:Blotting, Western; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003001:Cloning, Molecular; D003080:Cold Temperature; D017931:DNA Primers; D018552:Daucus carota / Q000737:chemistry*; D004587:Electrophoresis, Agar Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification*; D006031:Glycosylation; D015388:Organelles / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification
D021301:Antifreeze Proteins; D017931:DNA Primers; D006023:Glycoproteins; D011994:Recombinant Proteins