Spectrin interactions with globin chains in the presence of phosphate metabolites and hydrogen peroxide: implications for thalassaemia.
J Biosci
;
2007 Sep; 32(6): 1147-51
Article
in English
| IMSEAR
| ID: sea-110949
ABSTRACT
We 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.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Thalassemia
/
Humans
/
Globins
/
Sheep
/
Adenosine Triphosphate
/
Spectrin
/
2,3-Diphosphoglycerate
/
Protein Subunits
/
Hydrogen Peroxide
/
Animals
Language:
English
Journal:
J Biosci
Year:
2007
Type:
Article
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