Abstract
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 stilbenesensitive, protein was functionally involved in HCO -3 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 HCO -3 transport.
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Abbreviations
- AE1:
-
anion exchanger 1 (of red blood cells)
- CI:
-
inorganic carbon
References
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This paper is in partial fulfillment of a Ph.D. study by R. Sharkia. Supported by the Israel Academy of Sciences, grant 441/93 (to S.B.)
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Sharkia, R., Beer, S. & Cabantchik, Z.I. A membrane-located polypeptide of Ulva sp. which may be involved in HCO -3 uptake is recognized by antibodies raised against the human red-blood-cell anion-exchange protein. Planta 194, 247–249 (1994). https://doi.org/10.1007/BF00196394
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DOI: https://doi.org/10.1007/BF00196394