par Devogel, Myriam ;Polastro, Enrico ;Vincentelli, Jean
Référence Korean Journal of Biochemistry, 10, 1, page (1-7)
Publication Publié, 1978
Article révisé par les pairs
Résumé : By the use of fluorescence quenching measurements and sucrose gradient centrifugation, evidence is obtained on the binding and the interaction between hemoglobin and human erythrocytes spectrin. The interaction, characterized by a K(D) of 0.4 μM, at pH 7.2 is very sensitive to the pH, and specific of hemoglobin and spectrin in its native state. It is suggested that spectrin is one of the erythrocyte membrane components responsible for the observed ghost retention of hemoglobin.