Structures of antifreeze peptides from the antarctic eel pout, Austrolycicthys brachycephalus.
The antarctic eel pout, Austrolycicthys brachycephalus, synthesizes two predominant antifreeze peptides (AFPs) which, based on purification yields, make up about 94 and 6%, respectively, of the antifreezes in its serum. The amino acid sequences of these two AFPs, AB1 and AB2, were determined using automated sequencing, and compositional analyses of peptide fragments from enzymatic digests, and verified by molecular masses obtained with Fast Atom Bombardment Mass spectrometry. Substantial homologies in amino acid sequence exist between the AFPs of Austrolycicthys and those of other Southern and Northern eel pouts. 72% of the residues of AB1, and 84% of AB2, are identical to those of an AFP from another antarctic eel pout, Rhigophila dearborni. Between AB1 and AB2, 83% of the residues are identical. Secondary structure data based on circular dichroism studies indicated AB1 to be a random chain, but a sharp thermal transition of CD spectra around 30 degrees C suggested the presence of definite secondary or tertiary structure.
Cheng
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Department of Physiology and Biophysics, University of Illinois, Urbana 61801.
DeVries
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D000595:Amino Acid Sequence; D000818:Animals; D000864:Antarctic Regions; D021301:Antifreeze Proteins; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D005399:Fishes; D005615:Freezing; D006023:Glycoproteins / Q000302:isolation & purification; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D021301:Antifreeze Proteins; D006023:Glycoproteins