Record Display for the EPA National Library Catalog


Main Title Comparative Oxygen Affinity of Fish and Mammalian Myoglobins.
Author Nichols, J. W. ; Weber, L. J. ;
CORP Author Environmental Research Lab.-Duluth, MN. ;Oregon State Univ., Newport. Hatfield Marine Science Center.;National Inst. of Environmental Health Sciences, Research Triangle Park, NC.
Publisher c1989
Year Published 1989
Report Number EPA/600/J-89/287; NIEHS-ES-07060;
Stock Number PB90-196569
Additional Subjects Fishes ; Mammals ; Oxygen ; Myoglobin ; Graphs(Charts) ; Reprints ; Competitive binding ; Gel chromatography
Library Call Number Additional Info Location Last
NTIS  PB90-196569 Some EPA libraries have a fiche copy filed under the call number shown. 07/26/2022
Collation 7p
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 20 C, myoglobins from salmon and sculpin bound O2 with lower affinity than myoglobins from the rat or sperm whale. Oxygen binding studies at 12 C and 37 C 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 the study reveal a previously unrecognized diversity of myoglobin structure and function. (Copyright (c) 1989 Springer-Verlag.)