Properties of engineered antifreeze peptides.
Eight antifreeze-like peptides were produced by cleavage from engineered chimeric proteins. One was homologous to an antifreeze peptide of the winter flounder; the others differed in length and/or sequence. The homologous peptide and all those of equal or greater length were able to inhibit recrystallization. The longer peptides were so hydrophobic that their identification required modification of the usual protocols for high pressure liquid chromatography. Their elution positions were correlated to their hydrophobicities and their lengths. Additional naturally occurring antifreezes may be identifiable with this knowledge.
Warren
G J
GJ
DNA Plant Technology Corp., Oakland, CA 94608.
Hague
C M
CM
Corotto
L V
LV
Mueller
G M
GM
D000595:Amino Acid Sequence; D021301:Antifreeze Proteins; D002851:Chromatography, High Pressure Liquid; D003460:Crystallization; D003488:Cyanogen Bromide; D005615:Freezing; D006023:Glycoproteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D011487:Protein Conformation; D015202:Protein Engineering; D011993:Recombinant Fusion Proteins / Q000302:isolation & purification / Q000378:metabolism
D021301:Antifreeze Proteins; D006023:Glycoproteins; D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins; D003488:Cyanogen Bromide