Enzyme and hemoglobin retention in human erythrocyte stroma

The membrane association and dissociation of human glyceraldehyde‐3‐phosphate dehydrogenase under various conditions of hemolysis Immunochemical evidence for the lack of binding under cellular conditions

“…These results demonstrated the well-known effect of ionic strength on the GAPD-retention by human ghosts [5]. .…”

“…A dependence of protein binding to strome on ionic strength (O-75 mosm) and pH (5.4-8.2) was reported by Mitchell et al [5]. These authors concluded that the enzymes are not structurally important members of the membrane.…”

Investigations on the release of membrane‐bound glyceral‐dehyde‐3‐phosphate dehydrogenase

“…The sensibility of the GAPDH-membrane the enzyme. By reason of specific interaction between binding to electrolytes with an ionic strength greater NAD and the GAPDH molecule [ 11,121 it is assumed than 0.04 makes us assume electrostatic interactions that the releasing effect of NAD on membrane-bound between enzyme and membrane as already reported GAPDH is caused by such interaction, too, and not by other authors [3,7] .…”

Molecular sieving action of the cell membrane during gradual osmotic hemolysis

“…Nevertheless, Hb is reversibly bound to the cell membrane (Dodge, Mitchell and Hanahan, 1963;Mitchell, Mitchell and Hanahan, 1965;Duchon and Collier, 1971). Klipstein and Ranney (1960) found that human red cell membranes preferentially bound the most basic Hb that the cells contained (Hb A2 over A, S over A, and Cover S) but that rabbit RBC's, which do not contain a basic Hb, do not preferentially bind a specific Hb.…”