INTEC   05402
INSTITUTO DE DESARROLLO TECNOLOGICO PARA LA INDUSTRIA QUIMICA
Unidad Ejecutora - UE
artículos
Título:
SPIN LABEL STUDIES OF THE HEMOGLOBIN-MEMBRANE INTERACTION DURING SICKLE HEMOGLOBIN POLYMERIZATION
Autor/es:
J.E. FALCON; P.M. RODI; LORES M,; A. M. GENNARO
Revista:
APPLIED MAGNETIC RESONANCE
Editorial:
SPRINGER WIEN
Referencias:
Año: 2010 vol. 38 p. 443 - 453
ISSN:
0937-9347
Resumen:
An enhanced hemoglobin-membrane association has been previously documented in Sickle Cell Anemia.However, it is not known how this interaction is modified during the hemoglobin S polymerization process. Inthis work, we use a model of reconstituted erythrocytes from ghost membranes whose cytoskeleton proteinshad been previously labeled with the 4-maleimido Tempo spin label, and that were subsequently resealed withhemoglobin S or A solutions. Using EPR spectroscopy, we studied the time dependence of the spectral W/Sparameter, indicative of the conformational state of cytoskeleton proteins (mainly spectrin) under spontaneousdeoxygenation, with the aim of detecting the eventual effects due to hemoglobin S polymerization. Thedifferences observed in the temporal behaviour of W/S in erythrocytes reconstituted with both hemoglobinswere considered as experimental evidence of an increment in hemoglobin S-membrane interaction, as a resultof the polymerization process of hemoglobin S under spontaneous deoxygenation.