Identification of the phosphorylation site on human erythrocyte band 7 integral membrane protein: implications for a monotopic protein structure
U Salzer, H Ahorn, R Prohaska - Biochimica et Biophysica Acta (BBA) …, 1993 - Elsevier
U Salzer, H Ahorn, R Prohaska
Biochimica et Biophysica Acta (BBA)-Biomembranes, 1993•ElsevierBand 7 membrane protein was metabolically labelled with [32 P] phosphate in the presence
of cAMP, isolated and digested, the labelled peptides were purified and sequenced. Ser-9
was identified as the only phosphorylation site. This proves that the N-terminal region is
located at the cytoplasmic side of the membrane and implies a monotopic rather than the
predicted bitopic structure.
of cAMP, isolated and digested, the labelled peptides were purified and sequenced. Ser-9
was identified as the only phosphorylation site. This proves that the N-terminal region is
located at the cytoplasmic side of the membrane and implies a monotopic rather than the
predicted bitopic structure.
Abstract
Band 7 membrane protein was metabolically labelled with [32P]phosphate in the presence of cAMP, isolated and digested, the labelled peptides were purified and sequenced. Ser-9 was identified as the only phosphorylation site. This proves that the N-terminal region is located at the cytoplasmic side of the membrane and implies a monotopic rather than the predicted bitopic structure.
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