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Human erythrocyte band 3 polymorphism (band 3 Memphis): characterization of
the structural modification (Lys 56----Glu) by protein chemistry methods
D Yannoukakos, C Vasseur, C Driancourt, Y Blouquit, J Delaunay, H Wajcman and E Bursaux
Unite INSERM 299, Hopital de Bicetre, Le Kremlin-Bicetre, France.
Band 3 variants occur rather frequently in different populations. Based on
sodium dodecyl sulfate (SDS)-polyacrylamide electrophoretic properties, a
widespread polymorphism (band 3 Memphis) has been previously described. It
corresponds to a protein that has been hypothesized to be elongated in its
N-terminal cytoplasmic domain. Band 3 from a heterozygote subject for this
polymorphism and that displays a normal reactivity towards stilbene
disulfonates has been isolated and its primary structure determined by
protein chemistry. Reverse-phase high performance liquid chromatography
tryptic peptide mapping showed, as the only difference with controls, that
the enzymatic cleavage between the two N-terminal peptides did not occur,
yielding a 69 residue-long fragment. Further cleavages of this peptide
(cyanogen bromide, V8 protease), amino acid composition, and sequence
analyses demonstrated that the lysine at position 56 was replaced by a
glutamic acid. Thus, surprisingly, a single amino acid change is
responsible for the large difference in the electrophoretic behavior. This
result suggests that single amino acid substitutions may similarly be
involved in the structural modification of several other protein variants,
described as elongated or shortened based only on SDS-polyacrylamide
electrophoresis studies. When deletions/insertions were confirmed by
sequence analysis, their extent was often different from that expected from
electrophoresis.
Volume 78,
Issue 4,
pp. 1117-1120,
08/15/1991
Copyright © 1991 by The American Society of Hematology
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