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Identification by site-directed mutagenesis of Lys-558 as the covalent attachment site of H2DIDS in the mouse erythroid band 3 protein

✍ Scribed by Detlef Bartel; Heidrun Hans; Hermann Passow

Book ID: 115729113
Publisher: Elsevier Science
Year: 1989
Tongue: English
Weight: 280 KB
Volume: 985
Category: Article
ISSN: 0005-2736
DOI: 10.1016/0005-2736(89)90427-6

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✍ P. G. Wood; H. Müller; M. Sovak; H. Passow 📂 Article 📅 1992 🏛 Springer 🌐 English ⚖ 888 KB

The effect of mutation of either Lys 558 or Lys 869 or both on mouse erythroid band 3 protein (AE1)-mediated 36Cl- efflux and its inhibition by pyridoxal 5-phosphate (P5-P), DNDS and H2DIDS were studied. Regardless of the mutation, band 3 was always capable of executing Cl- self-exchange. P5-P (5 mM