Sialyltransferase acceptor activity of "antifreeze" glycoproteins from an antarctic fish

W. Thomas Shier; Gary Roloson

doi:10.1016/S0006-291X(74)80172-5

Sialyltransferase acceptor activity of "antifreeze" glycoproteins from an antarctic fish

W. Thomas Shier, Gary Roloson

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

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)
Pages (from-to)	51-56
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	59
Issue number	1
DOIs	https://doi.org/10.1016/S0006-291X(74)80172-5
State	Published - Jul 10 1974
Externally published	Yes

Bibliographical note

Funding Information:
Supported by grants AI 10265 and CA 14195 from the National Institutes of Health.

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10.1016/S0006-291X(74)80172-5

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title = "Sialyltransferase acceptor activity of {"}antifreeze{"} glycoproteins from an antarctic fish",

abstract = "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.",

author = "{Thomas Shier}, W. and Gary Roloson",

note = "Funding Information: Supported by grants AI 10265 and CA 14195 from the National Institutes of Health.",

year = "1974",

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doi = "10.1016/S0006-291X(74)80172-5",

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T1 - Sialyltransferase acceptor activity of "antifreeze" glycoproteins from an antarctic fish

AU - Thomas Shier, W.

AU - Roloson, Gary

N1 - Funding Information: Supported by grants AI 10265 and CA 14195 from the National Institutes of Health.

PY - 1974/7/10

Y1 - 1974/7/10

N2 - 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.

AB - 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.

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JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

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Sialyltransferase acceptor activity of "antifreeze" glycoproteins from an antarctic fish

Abstract

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