Fig. 8.
Fig. 8. Increased binding of HbS-Oman to normal (HbAA) Hb-stripped “leaky” RBC ghost membranes. SDS-PAGE (7.5% acrylamide), using the Fairbanks discontinuous buffer system, stained with Coomassie brilliant blue of purified HbAA or HbS-Oman incubated with normal (HbAA) Hb-stripped “leaky” RBC ghost membranes. Lane 1, normal (HbAA) Hb-stripped “leaky” ghosts; lane 2, 0.005 mg purified HbS-Oman; lanes 3 through 5, “leaky” ghosts incubated with HbAA; lanes 6 and 10, “leaky” ghosts without added Hb; lanes 7 through 9, “leaky” ghosts incubated with HbS-Oman. The position of band 3 and Hb is indicated. There was considerably more binding of HbS-Oman to “leaky” ghosts compared with the binding of HbAA.

Increased binding of HbS-Oman to normal (HbAA) Hb-stripped “leaky” RBC ghost membranes. SDS-PAGE (7.5% acrylamide), using the Fairbanks discontinuous buffer system, stained with Coomassie brilliant blue of purified HbAA or HbS-Oman incubated with normal (HbAA) Hb-stripped “leaky” RBC ghost membranes. Lane 1, normal (HbAA) Hb-stripped “leaky” ghosts; lane 2, 0.005 mg purified HbS-Oman; lanes 3 through 5, “leaky” ghosts incubated with HbAA; lanes 6 and 10, “leaky” ghosts without added Hb; lanes 7 through 9, “leaky” ghosts incubated with HbS-Oman. The position of band 3 and Hb is indicated. There was considerably more binding of HbS-Oman to “leaky” ghosts compared with the binding of HbAA.

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