Abstract
Enzymic digests of bovine hemoglobin were fractionated by reverse-phase liquid chromatography. The antifreeze activities of the fractions were analyzed by determing the amount of unfreezable water in their solutions. Fractions with high antifreeze activity were further purified by reverse- and normal-phase liquid chromatography. As the result, four peptides with high antifreeze activity were isolated. The amino acid sequences of them were identified as Gly-Gln-Ala-Gly-Ala, Val-Gly-Gly-Glu, Gly-Ser-Asp-Gln-Val-Lys and sodium salt of Ser-Ala-Glu-Glu. From the antifreeze activities of them and of commercial peptides, it is assumed that peptides mainly consisted of hydrophilic amino acids or low molecular weight amino acids and sodium salt of peptides mainly consisted of acidic amino acids have high antifreeze activities.
