Effects of domain-specific erythrocyte membrane modulators on acetylcholinesterase and NADH:Cytochrome b5 reductase activities

Donna A. Palmieri, Anuradha Rangachari, D. Allan Butterfield

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5 Scopus citations


Previously, we showed using electron paramagnetic resonance that the physical state of one side of erythrocyte membranes could be modulated by agents which interact with the opposite side (reviewed in Butterfield, 1989, Biological and Synthetic Membranes, A. R. Liss, Inc., New York). The present study was undertaken to determine whether membrane-bound enzymes would exhibit a similar transmembrane modulation effect. The effects of known, domain-specific modulators of the physical state of erythrocyte membranes on the activity of two membrane-bound enzymes were investigated. Acetylcholinesterase, an enzyme having its active site situated on the extracellular side of the membrane, seemed to be unaffected by most of the modulators employed in this study, with the exception of reversible inhibition by benzyl alcohol. Conversely, the activity of NADH:cytochrome b5 reductase, an enzyme whose active site is located on the cytoplasmic side of the erythrocyte membrane, was increased by those agents that interact primarily with skeletal proteins to increase skeletal protein-protein interactions; however, those agents which interact primarily with the skeleton to decrease protein-protein interactions decreased the activity of NADH:cytochrome b5 reductase. This enzyme's activity was also significantly altered by lectins which bind specifically to the external face of glycophorin A on the opposite side of the membrane, but it's activity was unaffected by concanavalin A, a lectin which binds to the external face of band 3. The results of these biochemical studies suggested that NADH:cytochrome b5 reductase can interact with and its activity can be modulated by skeletal or transmembrane proteins. In addition, these results support the hypothesis that in transmembrane signaling processes, biophysical and biochemical changes are correlated.

Original languageEnglish
Pages (from-to)224-228
Number of pages5
JournalArchives of Biochemistry and Biophysics
Issue number1
StatePublished - Jul 1990

Bibliographical note

Funding Information:
This work was supported in part by a grant from NSF 10671).

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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