Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Antifreeze proteins from the sea raven, Hemitripterus americanus. Further evidence for diversity among fish polypeptide antifreezes

Journal Article · · J. Biol. Chem.; (United States)
OSTI ID:5705590
The antifreeze proteins of the sea raven, Hemitripterus americanus, were isolated and compared with other fish antifreeze proteins. The sea raven contains one major protein of molecular weight 14,000-16,000 with little or no carbohydrate. Except for its similar seasonal appearance, the sea raven antifreeze protein differs from other polypeptide antifreeze in its amino acid composition, secondary structure, and immunological specificity. Amino acid analysis of sea raven antifreeze showed that it contains a high amount of half-cystine, hydrophilic amino acids, and only an average amount of alanine. In contrast, all other fish antifreeze proteins contain approximately 60% alanine and no half-cystine residues. Furthermore, the sea raven antifreeze protein is sensitive to sulfhydryl reagents. The antifreeze activity was decreased by 67% in the presence of 0.01 M dithiothreitol. Circular dichroism studies indicated the absence of significant amounts of ..cap alpha..-helix and the possible presence of ..beta..-structure. Antibodies raised against the antifreeze protein did not cross-react with the known polypeptide antifreeze from the winter flounder and shorthorn sculpin (Hew, C.L., Fletcher, G.L., and Ananthanarayanan, V.S. (1980) Can. J. Biochem. 58, 377-383). A specific radioimmunoassay was developed for the sea raven antifreeze protein and was used to quantitate the protein concentration in the fish. The seasonal profile obtained by radioimmunoassay was compatible with the antifreeze activity determined with a freezing point osmometer.
Research Organization:
Memorial Univ. of Newfoundland, St. John's, Canada
OSTI ID:
5705590
Journal Information:
J. Biol. Chem.; (United States), Journal Name: J. Biol. Chem.; (United States) Vol. 256:4; ISSN JBCHA
Country of Publication:
United States
Language:
English