Interactions of Na+ with haemoglobin-organic phosphate complexes.
Longitudinal and transverse relaxation times were measured in aqueous solutions containing haemoglobin and 2,3-bisphosphoglycerate and in dilute lysates of human erythrocytes. Analysis of the data in terms of calculated excess relaxation rates shows that Na+ interacts with the protein-organic phosphate complex. The comparable magnitude of the effect in the model system and in dilute lysate suggests that intracellular Na+ binds to the haemoglobin-bisphosphate complex. Results obtained with adenosine triphosphate and D-glucose indicate that there is also interaction between Na+ and haemoglobin complexes of these molecules.
Department of Biochemistry, University of Sydney, N.S.W., Australia.
G L
GL
Mendz
P W
PW
Kuchel
G R
GR
Wilcox
D019794:2,3-Diphosphoglycerate; D004163:Diphosphoglyceric Acids / Q000097:blood*; D004912:Erythrocytes / Q000378:metabolism; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008433:Mathematics; D011485:Protein Binding; D012964:Sodium / Q000097:blood*
D004163:Diphosphoglyceric Acids; D006454:Hemoglobins; D019794:2,3-Diphosphoglycerate; D012964:Sodium