COMPARATIVE OXYGEN AFFINITY OF FISH AND MAMMALIAN MYOGLOBINS

Myoglobins from rat, coho salmon (Oncorhynchus kisutch), buffalo sculpin (Enophrys bison) hearts, and yellowfin tuna (Thunnus albacares) red skeletal muscle were partially purified and their O2 binding affinities determined. Commercially prepared sperm whale myoglobin was employed as an internal sta...

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Main Authors: J.W. Nichols, L.J. Weber
Format: Text
Language:unknown
Published: 2005
Subjects:
Sperm whale
Online Access:http://oaspub.epa.gov/eims/eimsapi.dispdetail?deid=48257
id ftepa:oai:epaEIMS:48257
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spelling ftepa:oai:epaEIMS:48257 2023-05-15T18:26:34+02:00 COMPARATIVE OXYGEN AFFINITY OF FISH AND MAMMALIAN MYOGLOBINS J.W. Nichols L.J. Weber 2005-12-22T16:33:12Z http://oaspub.epa.gov/eims/eimsapi.dispdetail?deid=48257 unknown http://www.ntis.gov/search/product.asp?ABBR=PB90196569&starDB=GRAHIST Office of Research and Development Text 2005 ftepa 2007-11-21T13:47:57Z Myoglobins from rat, coho salmon (Oncorhynchus kisutch), buffalo sculpin (Enophrys bison) hearts, and yellowfin tuna (Thunnus albacares) red skeletal muscle were partially purified and their O2 binding affinities determined. Commercially prepared sperm whale myoglobin was employed as an internal standard. Tested at 20oC, myoglobins from salmon and sculpin bound O2 with lower affinity than myoglobins from the rat or sperm whale. Oxygen binding studies at 12oC and 37oC suggest that this difference is adaptive, permitting myoglobins from cold-adapted fish to function at physiologically relevant temperatures. Taken together, purification and O2, binding data obtained in this study reveal a previously unrecognized diversity of myoglobin structure and function. Text Sperm whale Environmental Protection Agency (EPA): Science Inventory
institution Open Polar
collection Environmental Protection Agency (EPA): Science Inventory
op_collection_id ftepa
language unknown
description Myoglobins from rat, coho salmon (Oncorhynchus kisutch), buffalo sculpin (Enophrys bison) hearts, and yellowfin tuna (Thunnus albacares) red skeletal muscle were partially purified and their O2 binding affinities determined. Commercially prepared sperm whale myoglobin was employed as an internal standard. Tested at 20oC, myoglobins from salmon and sculpin bound O2 with lower affinity than myoglobins from the rat or sperm whale. Oxygen binding studies at 12oC and 37oC suggest that this difference is adaptive, permitting myoglobins from cold-adapted fish to function at physiologically relevant temperatures. Taken together, purification and O2, binding data obtained in this study reveal a previously unrecognized diversity of myoglobin structure and function.
format Text
author J.W. Nichols
L.J. Weber
spellingShingle J.W. Nichols
L.J. Weber
COMPARATIVE OXYGEN AFFINITY OF FISH AND MAMMALIAN MYOGLOBINS
author_facet J.W. Nichols
L.J. Weber
author_sort J.W. Nichols
title COMPARATIVE OXYGEN AFFINITY OF FISH AND MAMMALIAN MYOGLOBINS
title_short COMPARATIVE OXYGEN AFFINITY OF FISH AND MAMMALIAN MYOGLOBINS
title_full COMPARATIVE OXYGEN AFFINITY OF FISH AND MAMMALIAN MYOGLOBINS
title_fullStr COMPARATIVE OXYGEN AFFINITY OF FISH AND MAMMALIAN MYOGLOBINS
title_full_unstemmed COMPARATIVE OXYGEN AFFINITY OF FISH AND MAMMALIAN MYOGLOBINS
title_sort comparative oxygen affinity of fish and mammalian myoglobins
publishDate 2005
url http://oaspub.epa.gov/eims/eimsapi.dispdetail?deid=48257
genre Sperm whale
genre_facet Sperm whale
op_source Office of Research and Development
op_relation http://www.ntis.gov/search/product.asp?ABBR=PB90196569&starDB=GRAHIST
_version_ 1766208540618260480

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