The alteration of the functional properties of human haemoglobin by spectrin.
Kinetic investigation by means of stopped flow techniques showed the rate of deoxygenation of haemoglobin to be slower in the presence of spectrin. At pH 7.15, the kinetic constant was 27.2 sec-1 in presence of spectrin instead of 34.3 sec-1 for haemoglobin alone. Also, equilibrium studies have revealed that the oxygen pressure for half-saturated haemoglobin decreased when spectrin was added to the reaction medium. At pH 7.35, the log (pO2)1/2 was 0.88 for haemoglobin in presence of spectrin instead of 0.93 for haemoglobin alone. From these results, an interaction between spectrin and haemoglobin may be suspected.
D006454:Hemoglobins; D006801:Humans; D007700:Kinetics; D008565:Membrane Proteins / Q000494:pharmacology*; D010100:Oxygen; D010108:Oxyhemoglobins; D011485:Protein Binding; D013049:Spectrin / Q000494:pharmacology*; D013053:Spectrophotometry
D006454:Hemoglobins; D008565:Membrane Proteins; D010108:Oxyhemoglobins; D013049:Spectrin; D010100:Oxygen