Figure 1: The profile of band 3 in the membranes of normal and CML erythrocytes. Western-blotted membrane proteins of erythrocytes (a–d) were stained with monoclonal anti-band 3 antibody. (a) The normal erythrocyte (N) shows the parent band 3 molecule at 95 kDa, and fragments at 55, 43, and below 26 kDa. (b–e) CML samples designated as “C” showed varied degree of fragmentation of band 3 as shown in (b) wherein parent band 3 is seen at 95 kDa and all fragments observed in normal are additionally cleaved (c) in which parent band 3 is not detected, and fragments detected in normal erythrocyte show greater intensity compared to the normal sample (d) where neither parent molecule nor the fragments are detected; (e) the fragments not detected in the representative CML sample in (d) are stained by polyclonal antibody to the whole band 3 molecule, thus indicating excessive cleavage of the N-terminal region which is detected by the monoclonal antibody.