The "antifreeze" glycoproteins from the Antarctic fish T. borchgrevinki function as effective acceptors for N-acetylneuraminic acid transfered from cytidine 5′-monophosphate N-acetylneuraminic acid by solublized enzymes from rat liver and a rat mammary adenocarcinoma. The properties of the two preparations are sufficiently similar to suggest that the same enzyme(s) are involved. The similarity between the glycoside structure that must result from this reaction and the known glycoside structures of some mucins and blood group substances invites the suggestion that the antifreeze glycoproteins were evolved during adaptation to a freezing environment by loss of the capability of transferring sialic acid to the antifreeze glycoprotein structure.
|Original language||English (US)|
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Jul 10 1974|
Bibliographical noteFunding Information:
Supported by grants AI 10265 and CA 14195 from the National Institutes of Health.