Structural stability of the erythrocyte anion transporter, band 3, in native membranes and in detergent micelles.

Journal article

The exothermic thermal denaturation transition of band 3, the anion transporter of the human erythrocyte membranes, has been studied by differential scanning calorimetry, in ghost membranes and in nonionic detergent micelles. In detergent micelles the transmembrane domain of band 3 gave an irreversible denaturation transition (C transition). However, no thermal transition was observed for the N-terminal cytoplasmic domain when band 3 was solubilised in detergent micelles. A reduction in entha...

Expand abstract

Authors: Sami, M; Malik, S; Watts, A

• Publication status: Published
• Journal: Biochimica et biophysica acta
• Volume: 1105
• Issue: 1
• Pages: 148-154
• Publication date: 1992-03-01
• DOI: 10.1016/0005-2736(92)90173-j
• ISSN: 0006-3002
• Language: English
• Keywords: Protein Conformation; Temperature; 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid; 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid; Detergents; Erythrocyte Membrane; Micelles; Protein Denaturation; Anion Exchange Protein 1, Erythrocyte; Humans; Calorimetry, Differential Scanning