Carbohydrate structure and serological behaviour of “antifreeze” glycoproteins from an antarctic fish

1975 ◽  
Vol 66 (2) ◽  
pp. 701-705 ◽  
Author(s):  
W.M. Glöckner ◽  
R.A. Newman ◽  
G. Yhlenbruck
Keyword(s):  
Antarctic Fish ◽  
Carbohydrate Structure ◽  
Antifreeze Glycoproteins

scholarly journals Antifreeze glycoproteins from Antarctic fish. Inactivation by borate.

1976 ◽  
Vol 251 (10) ◽  
pp. 3033-3036
Author(s):  
A I Ahmed ◽  
Y Yeh ◽  
Y Y Osuga ◽  
R E Feeney
Keyword(s):  
Antarctic Fish ◽  
Antifreeze Glycoproteins

Synthesis of an Isotopically-labelled Antarctic Fish Antifreeze Glycoprotein Probe

2011 ◽  
Vol 64 (6) ◽  
pp. 723 ◽  
Author(s):  
Joanna M. Wojnar ◽  
Clive W. Evans ◽  
Arthur L. DeVries ◽  
Margaret A. Brimble
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Building Block ◽  
Exocrine Pancreas ◽  
Antarctic Fish ◽  
Antifreeze Glycoproteins ◽  
Threonine Residue ◽  
Antarctic Fishes ◽  
Antifreeze Glycoprotein ◽  
Acid Unit

Antifreeze glycoproteins (AFGPs) are glycosylated polypeptides produced by Antarctic and Arctic fishes, which allow them to survive in seawater at sub-zero temperatures. An investigation into the postulated enteric uptake of AFGP synthesized in the exocrine pancreas of Antarctic fishes required a custom-prepared AFGP probe that incorporated seven isotopically-labelled Ala residues for detection by mass spectrometry. The AFGPs are composed of a repetitive three amino acid unit (Ala-Ala-Thr), in which the threonine residue is glycosylated with the disaccharide β-d-Gal-(1→3)-α-d-GalNAc. The synthesis of isotopically-labelled AFGP8 (1), as well as the optimized synthesis of the protected glycosylated amino acid building block 2, is reported.

scholarly journals Comparison of the Solution Conformation and Dynamics of Antifreeze Glycoproteins from Antarctic Fish

2000 ◽  
Vol 78 (6) ◽  
pp. 3195-3207 ◽  
Author(s):  
Andrew N. Lane ◽  
Lisa M. Hays ◽  
Nelly Tsvetkova ◽  
Robert E. Feeney ◽  
Lois M. Crowe ◽  
...  
Keyword(s):  
Antarctic Fish ◽  
Solution Conformation ◽  
Antifreeze Glycoproteins

Fish Antifreeze Glycoproteins Protect Cellular Membranes During Lipid-Phase Transitions

Physiology ◽  
1997 ◽  
Vol 12 (4) ◽  
pp. 189-194
Author(s):  
LM Hays ◽  
RE Feeney ◽  
F Tablin ◽  
AE Oliver ◽  
NJ Walker ◽  
...  
Keyword(s):  
Lipid Bilayers ◽  
Liquid Crystalline ◽  
Antarctic Fish ◽  
Cell Types ◽  
Lipid Phase ◽  
Crystal Formation ◽  
Ice Crystal ◽  
Antifreeze Glycoproteins ◽  
Lipid Phase Transitions ◽  
Gel Phase

Antifreeze proteins from Antarctic fish depress solution freezing temperatures, inhibit ice crystal formation, and prevent recrystallization on rewarming. They have been used to enhance survival of some cell types during hypothermic storage. The mechanism of their protection is thought to be important during the transition of lipid bilayers from a liquid crystalline to a gel phase.

Structure of the carbohydrate of antifreeze glycoproteins from an antarctic fish

FEBS Letters ◽  
1975 ◽  
Vol 54 (2) ◽  
pp. 135-138 ◽  
Author(s):  
W.Thomas Shier ◽  
Yuan Lin ◽  
Arthur L. DeVries
Keyword(s):  
Antarctic Fish ◽  
Antifreeze Glycoproteins

scholarly journals Antifreeze glycoproteins from the blood of an antarctic fish. The structure of the proline-containing glycopeptides.

1978 ◽  
Vol 253 (14) ◽  
pp. 5155-5162
Author(s):  
H.R. Morris ◽  
M.R. Thompson ◽  
D.T. Osuga ◽  
A.I. Ahmed ◽  
S.M. Chan ◽  
...  
Keyword(s):  
Antarctic Fish ◽  
Antifreeze Glycoproteins

Preparation and galactosyltransferase acceptor activity of derivatives of antifreeze glycoproteins of an Antarctic fish

1977 ◽  
Vol 55 (8) ◽  
pp. 886-893 ◽  
Author(s):  
W. Thomas Shier ◽  
Gary J. Roloson
Keyword(s):  
Rat Liver ◽  
Liver Microsomes ◽  
Antarctic Fish ◽  
Helical Structure ◽  
Structural Features ◽  
Rat Liver Microsomes ◽  
Antifreeze Glycoproteins ◽  
Galactosyl Transferase ◽  
Acceptor Activity ◽  
The Antarctic

A series of 12 closely related glycoproteins containing α-linked N-acetyl-D-galactosamine (GalNAc) as the sole carbohydrate moiety have been prepared by degradation of the antifreeze glycoproteins from the serum of the Antarctic fish Trematomus borchgrevinki. The polypeptide moieties of these glycoproteins contain substitutions in the normal -Ala-Ala-Thr- repeating tripeptide sequence which introduce alterations in the amount of α-helical structure and the density of acceptor sites, and theoretically also in the amount of rigidity, polarity, and hydrophobicity of the polypeptide. Of these alterations only density of acceptor sites has a statistically significant effect on the ability of the [Formula: see text] moiety to act as a substrate for galactosyl-transferase (EC 2.4.1.22) activity solubilized from rat liver microsomes. This result suggests that in the biosynthesis of rat liver glycoproteins these structural features of the polypeptide moiety of glycoproteins are not part of the substrate specificity of the galactosyltransferase activity that transfers the second monosaccharide. Hence, these structural features do not play a major role in determining the structure of the threonine-linked oligosaccharide after its synthesis has been initiated.

Water binding by antifreeze glycoproteins from Antarctic fish

Nature ◽  
1977 ◽  
Vol 269 (5623) ◽  
pp. 87-88 ◽  
Author(s):  
A. E. V. HASCHEMEYER ◽  
W. GUSCHLBAUER ◽  
ARTHUR L. DEVRIES
Keyword(s):  
Antarctic Fish ◽  
Antifreeze Glycoproteins ◽  
Water Binding
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