Cat hemoglobin: pH-dependent cooperativity of oxygen binding.
Cat hemoglobin has a lower cooperativity and oxygen affinity than most mammalian hemoglobins. In contrast to the usual invariance of cooperativity with pH, a rise in cooperativity with pH is predicted by the allosteric model for low-affinity hemoglobins. Such a pH-dependent cooperativity for cat hemoglobin has been found.
D000818:Animals; D002415:Cats; D006454:Hemoglobins / Q000032:analysis / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010100:Oxygen / Q000097:blood*; D011487:Protein Conformation; D013053:Spectrophotometry
D006454:Hemoglobins; D010100:Oxygen