| First Author | Kang D | Year | 1994 |
| Journal | Biochim Biophys Acta | Volume | 1194 |
| Issue | 2 | Pages | 341-4 |
| PubMed ID | 7522566 | Mgi Jnum | J:20893 |
| Mgi Id | MGI:68957 | Doi | 10.1016/0005-2736(94)90317-4 |
| Citation | Kang D, et al. (1994) Anion transport function of mouse erythroid band 3 protein (AE1) does not require acylation of cysteine residue 861. Biochim Biophys Acta 1194(2):341-4 |
| abstractText | Cys-861 of mouse band 3 is equivalent to Cys-843 of human band 3, the only acylated cysteine residue in the anion exchanger AE1 of the red blood cell (Hamasaki et al. (1992) Progress Cell Res. 2, 65-71). Mutation of Cys-861 to serine or methionine caused no significant changes of band 3-mediated anion exchange as measured after expression of the appropriate cRNAs in Xenopus oocytes. Susceptibility to inhibition of transport by 4,4'-dinitrostilbene-2,2'-disulfonate and PCMBS was not affected. We conclude that palmitoylation is not an absolute requirement for the successful execution the anion transport function by the hydrophobic domain of band 3 in the plasma membrane. |
