Antifreeze Glycopeptides of Antarctic Fish: Comparative Aspects of Their Biochemistry and Physiology

124 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1987. The presence of antifreeze glycopeptides (AFGPs) in the blood of polar fishes allows fish to live in ice-laden seawater at a temperature below what colligative properties would dicate to be the freezing point of their blood. AF...

Full description

Bibliographic Details
Main Author: Ahlgren, Jeffrey Allen
Format: Text
Language:unknown
Published: 1987
Subjects:
Online Access:http://hdl.handle.net/2142/77684
id ftunivillidea:oai:www.ideals.illinois.edu:2142/77684
record_format openpolar
spelling ftunivillidea:oai:www.ideals.illinois.edu:2142/77684 2023-05-15T13:33:27+02:00 Antifreeze Glycopeptides of Antarctic Fish: Comparative Aspects of Their Biochemistry and Physiology Ahlgren, Jeffrey Allen 1987 http://hdl.handle.net/2142/77684 unknown http://hdl.handle.net/2142/77684 (UMI)AAI8711765 Chemistry Biochemistry text 1987 ftunivillidea 2016-03-19T23:48:28Z 124 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1987. The presence of antifreeze glycopeptides (AFGPs) in the blood of polar fishes allows fish to live in ice-laden seawater at a temperature below what colligative properties would dicate to be the freezing point of their blood. AFGPs are well-characterized from two antarctic species, Pagothenia borchgrevinki and Dissostichus mawsoni. Eight other species of antarctic fish were examined for AFGPs, and results showed a high degree of similarity of AFGP between species. ('3)H AFGP was prepared and injected in the blood of the antarctic nototheniid fish Trematomus bernacchii, and the results showed that body fluids which are blood filtrates, including the interstitial fluid of all tissues except brain, contain all AFGPs, while fluids formed by secretory processes lack AFGP and are supercooled at environmental temperatures (-1.9(DEGREES)C). Skin from the antarctic fish Gymnodraco acuticepts was shown to prevent ice propagation into supercooled saline at environmental temperatures, demonstrating the role of extracellular AFGP in the prevention of ice propagation. The amino acid proline, which is present in the peptide portion of all low molecular weight AFGPs examined to date, was shown to enhance the rate of glycosylation by 10-fold of deglycosylated low molecular weight AFGP in vitro by comparing the rates of glycosylation of proline-containing and proline-free low molecular weight deglycosylated AFGP. Text Antarc* Antarctic University of Illinois at Urbana-Champaign: IDEALS (Illinois Digital Environment for Access to Learning and Scholarship) Antarctic The Antarctic
institution Open Polar
collection University of Illinois at Urbana-Champaign: IDEALS (Illinois Digital Environment for Access to Learning and Scholarship)
op_collection_id ftunivillidea
language unknown
topic Chemistry
Biochemistry
spellingShingle Chemistry
Biochemistry
Ahlgren, Jeffrey Allen
Antifreeze Glycopeptides of Antarctic Fish: Comparative Aspects of Their Biochemistry and Physiology
topic_facet Chemistry
Biochemistry
description 124 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1987. The presence of antifreeze glycopeptides (AFGPs) in the blood of polar fishes allows fish to live in ice-laden seawater at a temperature below what colligative properties would dicate to be the freezing point of their blood. AFGPs are well-characterized from two antarctic species, Pagothenia borchgrevinki and Dissostichus mawsoni. Eight other species of antarctic fish were examined for AFGPs, and results showed a high degree of similarity of AFGP between species. ('3)H AFGP was prepared and injected in the blood of the antarctic nototheniid fish Trematomus bernacchii, and the results showed that body fluids which are blood filtrates, including the interstitial fluid of all tissues except brain, contain all AFGPs, while fluids formed by secretory processes lack AFGP and are supercooled at environmental temperatures (-1.9(DEGREES)C). Skin from the antarctic fish Gymnodraco acuticepts was shown to prevent ice propagation into supercooled saline at environmental temperatures, demonstrating the role of extracellular AFGP in the prevention of ice propagation. The amino acid proline, which is present in the peptide portion of all low molecular weight AFGPs examined to date, was shown to enhance the rate of glycosylation by 10-fold of deglycosylated low molecular weight AFGP in vitro by comparing the rates of glycosylation of proline-containing and proline-free low molecular weight deglycosylated AFGP.
format Text
author Ahlgren, Jeffrey Allen
author_facet Ahlgren, Jeffrey Allen
author_sort Ahlgren, Jeffrey Allen
title Antifreeze Glycopeptides of Antarctic Fish: Comparative Aspects of Their Biochemistry and Physiology
title_short Antifreeze Glycopeptides of Antarctic Fish: Comparative Aspects of Their Biochemistry and Physiology
title_full Antifreeze Glycopeptides of Antarctic Fish: Comparative Aspects of Their Biochemistry and Physiology
title_fullStr Antifreeze Glycopeptides of Antarctic Fish: Comparative Aspects of Their Biochemistry and Physiology
title_full_unstemmed Antifreeze Glycopeptides of Antarctic Fish: Comparative Aspects of Their Biochemistry and Physiology
title_sort antifreeze glycopeptides of antarctic fish: comparative aspects of their biochemistry and physiology
publishDate 1987
url http://hdl.handle.net/2142/77684
geographic Antarctic
The Antarctic
geographic_facet Antarctic
The Antarctic
genre Antarc*
Antarctic
genre_facet Antarc*
Antarctic
op_relation http://hdl.handle.net/2142/77684
(UMI)AAI8711765
_version_ 1766042407488454656