Datta, PoppyChakrabarty, SudipaChakrabarty, AmitChakrabarti, Abhijit2007-09-242009-06-012007-09-242009-06-012007-09-24Datta P, Chakrabarty S, Chakrabarty A, Chakrabarti A. Spectrin interactions with globin chains in the presence of phosphate metabolites and hydrogen peroxide: implications for thalassaemia. Journal of Biosciences. 2007 Sep; 32(6): 1147-51http://imsear.searo.who.int/handle/123456789/110949We have shown the differential interactions of the erythroid skeletal protein spectrin with the globin subunits of adult haemoglobin (HbA); these indicate a preference for alpha-globin over that for beta-globin and intact HbA in an adenosine 5'-triphosphate (ATP)-dependent manner. The presence of Mg/ATP led to an appreciable decrease in the binding affinity of the alpha-globin chain to spectrin and the overall yield of globin-spectrin cross-linked complexes formed in the presence of hydrogen peroxide. Similar effects were also seen in the presence of 2-,3-diphosphoglycerate (2,3 DPG), the other important phosphate metabolite of erythrocytes. The binding affinity and yield of cross-linked high molecular weight complexes (HMWCs) formed under oxidative conditions were significantly higher in alpha-globin compared with intact haemoglobin, HbA and the beta-globin chain. The results of this study indicate a possible correlation of the preferential spectrin binding of the alpha-globin chain over that of the beta-globin in the haemoglobin disorder beta-thalassaemia.eng2,3-Diphosphoglycerate --bloodAdenosine Triphosphate --bloodAnimalsGlobins --metabolismHumansHydrogen Peroxide --bloodProtein Subunits --bloodSheepSpectrin --metabolismThalassemia --bloodJournal Article