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J. Biol. Chem., Vol. 266, Issue 27, 17826-17831, Sep, 1991
D Wang, WC Mentzer, T Cameron and RM Johnson
A 31-kDa human erythrocyte integral protein, band 7.2b, has been purified
to better than 95% homogeneity. The polypeptide was found to be insoluble
in most detergents and was isolated in denatured form by gel filtration in
the presence of sodium dodecyl sulfate and preparative electrophoresis. In
intact erythrocytes that were equilibrated with 32Pi, band 7.2b was
phosphorylated in response to exogenous dibutyryl cAMP. The peptide is also
palmitylated, as shown by its incorporation of radioactivity when intact
erythrocytes were incubated with [9,10-3H]palmitic acid. Antisera to band
7.2b were raised in rabbits, and these antibodies cross-react with 31-kDa
polypeptides in human liver and kidney. Immunoblots of red cells from a
number of other species were negative, with the exception of a cross-
reacting 23-kDa polypeptide in rat erythrocyte membranes. Band 7.2b was
absent in erythrocyte membranes from an individual with overhydrated
hereditary stomatocytes.
Purification of band 7.2b, a 31-kDa integral phosphoprotein absent in hereditary stomatocytosis
Department of Biochemistry, Wayne Street University, Detroit, Michigan 48201.
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