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

• Published in: Planta 1994, Vol.194 (2), p.247-249
• Main Authors: Sharkia, R, Beer, S, Cabantchik, Z.I
• Format: Article
• Language: English
• Subjects: active transport; animal proteins; Anion Exchange Protein 1, Erythrocyte - analysis; anions; Antibodies; bicarbonates; Bicarbonates - metabolism; Biotechnology; Blotting, Western; carbon; Cell Membrane - metabolism; Chlorophycota; cross reaction; Cross Reactions; Electrophoresis, Polyacrylamide Gel; Erythrocyte Membrane - metabolism; erythrocytes; Humans; ion transport; Membrane Proteins - analysis; Membrane Proteins - immunology; Membrane Proteins - isolation & purification; plant proteins; plasma membrane; polypeptides; Seaweed - metabolism
• ISSN: 0032-0935; 1432-2048
• DOI: 10.1007/BF00196394

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.