Nuclear Magnetic resonance quadrupole relaxation studies of chloride binding to the isolated hemoglobins from trout (Salmo irideus).
NMR studies of chloride binding to the main components of trout blood, Hb Trout I and Hb Trout IV, indicate that although the affinity of chloride is high for both hemoglobins, the characteristics of the binding process are markedly differnet. In Hb Trout IV chemical exchange at the chloride binding site(s) is fast and quadrupole effects determine the linewidth; chloride binding has a definite pH dependence, but there is no significant oxygen linkage. In contrast Hb Trout I represents a unique case of slow chemical exchange, which may depend on unusual stereoche mical characteristics of the chloride binding site; chloride binding is pH independent, but shows a significant oxygen linkage, which may be attributed to changes of the lifetime of chloride at the binding site. The chloride binding properties displayed by Hb Trout I and IV have been compared with those of normal and modified human hemoglobins and discussed in terms of the structural differences in the C- and N-terminal regions of the alpha- and beta-chains.
D000818:Animals; D001665:Binding Sites; D002712:Chlorides; D004112:Dimercaprol; D004492:Edetic Acid; D006454:Hemoglobins; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D008433:Mathematics; D010833:Phytic Acid; D011485:Protein Binding; D011487:Protein Conformation; D013696:Temperature; D014337:Trout
D002712:Chlorides; D006454:Hemoglobins; D004112:Dimercaprol; D010833:Phytic Acid; D004492:Edetic Acid