Hemoglobin and oxygen: different affinities in two species of rodents (Mus musculus and Pitymys duodecimcostatus).
Five different hemoglobins have been demonstrated by polyacrylamide-gel disk electrophoresis in the species Mus musculus. Oxygen affinities of hemoglobin (P50) from Mus musculus and Pitymys duodecimcostatus hemolysates were determined at pH 7.4 and 37 degrees C. Values obtained for delta log P50/delta pH in hemolysates from both species point out a more pronounced Bohr effect in Pitymys duodecimcostatus.
D000818:Animals; D003411:Arvicolinae / Q000097:blood*; D004591:Electrophoresis, Polyacrylamide Gel; D006454:Hemoglobins / Q000302:isolation & purification / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D051379:Mice / Q000097:blood*; D010100:Oxygen / Q000097:blood*; D010108:Oxyhemoglobins / Q000378:metabolism; D012377:Rodentia / Q000097:blood*; D013045:Species Specificity
D006454:Hemoglobins; D010108:Oxyhemoglobins; D010100:Oxygen