The interaction of adenine nucleotides with the red cell membrane: A calorimetric study

Philip S. Low, John F. Brandts

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

The interaction of two adenine nucleotides with the red cell membrane was investigated using highly sensitive differential scanning calorimetry. It was found that ADP and AMP-PNP (an ATP analogue) preferentially modify the A transition, which has been shown to involve the unfolding of a portion of spectrin, an erythrocyte membrane protein complex. The interaction of ADP with spectrin was shown to be reversible and facilitated by the usual cofactor, Mg2+. The ADP-induced modification, however, is only observed for membrane associated spectrin; ADP has no effect on extracted spectrin. The results presented are consistent with an ADP-induced conformational change in the spectrin complex which leads to a change in the spectrin-membrane interaction. ADP, but not AMP-PNP, is shown to modify an additional calorimetric transition (B2) associated with a structural change in the transmembrane protein band 3. This behavior is characteristic of inhibitors of anion transport in the red cell. ADP is also found to be an inhibitor of anion transport in red cells.

Original languageEnglish (US)
Pages (from-to)640-646
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume190
Issue number2
DOIs
StatePublished - Oct 1978

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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