Heterogeneity in the human erythrocyte Band 3 anion-transporter revealed by Triton X-114 phase partitioning

M. L. Swanson, R. K. Keast, M. L. Jennings, J. E. Pessin

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6 Scopus citations


Triton X-114 phase partitioning used in conjunction with countercurrent distribution was utilized to examine the phasing properties of the human erythrocyte Band 3 anion-transport protein. Phase partitioning and countercurrent distribution of Band 3 protein followed by electrophoresis and immunoblotting revealed that Band 3 protein possesses biphasic properties with approx. 65% of the Band 3 97,000-M(r) species being localized in the detergent phase and 35% isolated in the aqueous phase. The bidirectional phasing of the anion-transporter does not appear to be a result of glycosylation or phosphorylation, since treatment of alkali-washed ghosts with glycosidases or phosphatase respectively did not significantly alter the phasing profiles. Chymotrypsin treatment of erythrocytes followed by the purification of the 60,000-M(r) fragment, and exposure of this fragment to phase separation and countercurrent distribution also revealed biphasic partitioning with 70% of the species being isolated in the aqueous phase and 30% in the detergent phase. These data demonstrate that the human erythrocyte Band 3 anion-transport protein is heterogeneous by Triton X-114 phase partitioning and that this heterogeneity is preserved in the 60,000-M(r) chymotryptic fragment of Band 3 protein.

Original languageEnglish (US)
Pages (from-to)229-234
Number of pages6
JournalBiochemical Journal
Issue number1
Publication statusPublished - Jan 1 1988
Externally publishedYes


ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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