| Autor: |
Swanson ML; Department of Physiology and Biophysics, University of Iowa, Iowa City 52242., Keast RK, Jennings ML, Pessin JE |
| Jazyk: |
angličtina |
| Zdroj: |
The Biochemical journal [Biochem J] 1988 Oct 01; Vol. 255 (1), pp. 229-34. |
| Abstrakt: |
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-Mr 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-Mr 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 heterogenous by Triton X-114 phase partitioning and that this heterogeneity is preserved in the 60,000-Mr chymotryptic fragment of Band 3 protein. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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