Isopiestic determination of water binding by fish antifreeze glycoproteins

John G. Duman; Jean L. Patterson; John J. Kozak; Arthur L. DeVries

doi:10.1016/0005-2795(80)90127-0

Isopiestic determination of water binding by fish antifreeze glycoproteins

John G. Duman, Jean L. Patterson, John J. Kozak, Arthur L. DeVries

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

2 Scopus citations

Abstract

The effectiveness of water binding of antifreeze glycoproteins relative to hemoglobin, cytochrome c and polyvinylpyrrolidone was determined by analyzing results obtained in an isopiestic study at 25°C. The net weight of water which moved from a protein/NaCl aqueous sample to a saturated NaCl reference solution increased in the order: antifreeze glycoprotein, hemoglobin, polyvinylpyrrolidone and cytochrome c. Since the glycoproteins were least effective in transporting water we conclude that, of the proteins studied, the glycoprotein was most effective in binding water under equilibrium conditions at 25°C.

Original language	English (US)
Pages (from-to)	332-336
Number of pages	5
Journal	BBA - Protein Structure
Volume	626
Issue number	2
DOIs	https://doi.org/10.1016/0005-2795(80)90127-0
State	Published - Dec 16 1980

Keywords

(Fish)
Antifreeze glycoprotein
Isopiestic study
Water binding

ASJC Scopus subject areas

Medicine(all)

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10.1016/0005-2795(80)90127-0

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title = "Isopiestic determination of water binding by fish antifreeze glycoproteins",

abstract = "The effectiveness of water binding of antifreeze glycoproteins relative to hemoglobin, cytochrome c and polyvinylpyrrolidone was determined by analyzing results obtained in an isopiestic study at 25°C. The net weight of water which moved from a protein/NaCl aqueous sample to a saturated NaCl reference solution increased in the order: antifreeze glycoprotein, hemoglobin, polyvinylpyrrolidone and cytochrome c. Since the glycoproteins were least effective in transporting water we conclude that, of the proteins studied, the glycoprotein was most effective in binding water under equilibrium conditions at 25°C.",

keywords = "(Fish), Antifreeze glycoprotein, Isopiestic study, Water binding",

author = "Duman, {John G.} and Patterson, {Jean L.} and Kozak, {John J.} and DeVries, {Arthur L.}",

note = "Funding Information: This study was supported by NSF Grant PCM 77-03475 to J.G.D. and by NSF Grant PCM77-25166 A01 to A.L.D.",

year = "1980",

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language = "English (US)",

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TY - JOUR

T1 - Isopiestic determination of water binding by fish antifreeze glycoproteins

AU - Duman, John G.

AU - Patterson, Jean L.

AU - Kozak, John J.

AU - DeVries, Arthur L.

N1 - Funding Information: This study was supported by NSF Grant PCM 77-03475 to J.G.D. and by NSF Grant PCM77-25166 A01 to A.L.D.

PY - 1980/12/16

Y1 - 1980/12/16

N2 - The effectiveness of water binding of antifreeze glycoproteins relative to hemoglobin, cytochrome c and polyvinylpyrrolidone was determined by analyzing results obtained in an isopiestic study at 25°C. The net weight of water which moved from a protein/NaCl aqueous sample to a saturated NaCl reference solution increased in the order: antifreeze glycoprotein, hemoglobin, polyvinylpyrrolidone and cytochrome c. Since the glycoproteins were least effective in transporting water we conclude that, of the proteins studied, the glycoprotein was most effective in binding water under equilibrium conditions at 25°C.

AB - The effectiveness of water binding of antifreeze glycoproteins relative to hemoglobin, cytochrome c and polyvinylpyrrolidone was determined by analyzing results obtained in an isopiestic study at 25°C. The net weight of water which moved from a protein/NaCl aqueous sample to a saturated NaCl reference solution increased in the order: antifreeze glycoprotein, hemoglobin, polyvinylpyrrolidone and cytochrome c. Since the glycoproteins were least effective in transporting water we conclude that, of the proteins studied, the glycoprotein was most effective in binding water under equilibrium conditions at 25°C.

KW - (Fish)

KW - Antifreeze glycoprotein

KW - Isopiestic study

KW - Water binding

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JO - BBA - Protein Structure

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ER -

Isopiestic determination of water binding by fish antifreeze glycoproteins

Abstract

Keywords

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