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...

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Main Author: Ahlgren, Jeffrey Allen
Format: Text
Language:English
Published: 2015
Subjects:
geo
Online Access:http://hdl.handle.net/2142/77684
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spelling fttriple:oai:gotriple.eu:http://hdl.handle.net/2142/77684 2023-05-15T13:41:39+02:00 Antifreeze Glycopeptides of Antarctic Fish: Comparative Aspects of Their Biochemistry and Physiology Ahlgren, Jeffrey Allen 2015-05-14 http://hdl.handle.net/2142/77684 en eng (UMI)AAI8711765 http://hdl.handle.net/2142/77684 undefined IDEALS envir geo Text https://vocabularies.coar-repositories.org/resource_types/c_18cf/ 2015 fttriple 2023-01-22T17:05:22Z 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. U of I Only Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Text Antarc* Antarctic Unknown Antarctic The Antarctic
institution Open Polar
collection Unknown
op_collection_id fttriple
language English
topic envir
geo
spellingShingle envir
geo
Ahlgren, Jeffrey Allen
Antifreeze Glycopeptides of Antarctic Fish: Comparative Aspects of Their Biochemistry and Physiology
topic_facet envir
geo
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. U of I Only Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs
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 2015
url http://hdl.handle.net/2142/77684
geographic Antarctic
The Antarctic
geographic_facet Antarctic
The Antarctic
genre Antarc*
Antarctic
genre_facet Antarc*
Antarctic
op_source IDEALS
op_relation (UMI)AAI8711765
http://hdl.handle.net/2142/77684
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