Related Experiment Video
Updated: Aug 16, 2026

Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification
Published on: May 5, 2017
Type I antifreeze proteins: possible origins from chorion and keratin genes in Atlantic snailfish
Robert P Evans1, Garth L Fletcher
1Ocean Sciences Centre, Memorial University of Newfoundland, St. John's, Newfoundland A1C 5S7, Canada. robert.evans@ualberta.ca
Abstract:
Type I antifreeze proteins (AFPs) are alanine-rich alpha-helical polypeptides found in some species of right-eye flounders, sculpin, and snailfish. In this study, a shorthorn sculpin skin type I cDNA clone was used to probe an Atlantic snailfish liver cDNA library in order to locate expressed genes corresponding to snailfish plasma AFPs. Clones isolated from the cDNA library had sections with substantial amino acid and nucleotide sequence similarity to snailfish type I AFPs. However, further analysis revealed that the positives were actually three different liver-expressed proteins-two were eggshell proteins, while the third was a type II keratin. We propose that a shift in reading frame could produce alanine-rich candidate AFPs with possible antifreeze activity or ice crystal modification properties. Furthermore, it is plausible that one or more of the liver-expressed proteins represent the progenitors of snailfish type I AFPs.

