A membrane-located polypeptide of Ulva sp. which may be involved in HCO3- uptake is recognized by antibodies raised against the human red-blood-cell anion-exchange protein.
Polypeptides present in a membrane fraction of the marine macroalga Ulva sp. were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and tested for cross-reactivity with antibodies raised against the human red-blood-cell anion exchanger (AE1). A polypeptide of ca. 95 kDa was identified with a monoclonal, as well as two polyclonal (one against the C-terminus and one against the whole protein) antibodies, indicating that it shares homologous domains with AE1. These findings complement an earlier study which indicated that a plasmalemma-bound, disulfonic stilbene-sensitive, protein was functionally involved in HCO3- transport into the photosynthesizing cells of Ulva (Z. Drechsler et al. 1993, Planta 191, 34-40). It is thus suggested here that a similar protein has evolved, and has been conserved, in marine photosynthetic organisms and mammalian red blood cells for the purpose of HCO3- transport.
Sharkia
R
R
Department of Botany, Tel Aviv University, Israel.
Beer
S
S
Cabantchik
Z I
ZI
D001457:Anion Exchange Protein 1, Erythrocyte / Q000032:analysis*; D000906:Antibodies; D001639:Bicarbonates / Q000378:metabolism*; D015153:Blotting, Western; D002462:Cell Membrane / Q000378:metabolism; D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000032:analysis* / Q000276:immunology / Q000302:isolation & purification; D012624:Seaweed / Q000378:metabolism*
D001457:Anion Exchange Protein 1, Erythrocyte; D000906:Antibodies; D001639:Bicarbonates; D008565:Membrane Proteins