Binding of spectrin to hereditary spherocyte membranes

Steven R. Goodman, Scott A. Weidner, M. Elaine Eyster, Joseph J. Kesselring

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2 Scopus citations


The structural instability of red cells from hereditary spherocytic patients suggests that the primary molecular alteration in this disorder resides in the spectrin membrane skeleton, a macromolecular structure thought to control red cell shape. In this study, the protein composition of HS red cell ghosts, spectrin-depleted inverted vesicles, and spectrin heterodimers was quantitatively normal in 9 HS patients from 3 unrelated families. The binding of 32P-spectrin heterodimers to spectrin-depleted inverted vesicles (physiological ionic strength, pH 7.5, 4°C) indicated a KD of 18.6 ± 2.0 nm (mean ± s.e.) and a maximal binding capacity of 98 ± 7 μg of spectrin bound/mg of inverted vesicle protein for 9 HS patients, and 18.3 ± 1.8 nm and 116 ± 8 μg spectrin/mg of inverted vesicle protein in 9 paired normal controls. Therefore the binding of spectrin to the syndeins (Bands 2.1 → 2.6) its high affinity membrane binding site, is unaltered in hereditary spherocytosis.

Original languageEnglish (US)
Pages (from-to)91-97
Number of pages7
JournalJournal of Molecular and Cellular Cardiology
Issue numberSUPPL. 3
StatePublished - Sep 1982

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cardiology and Cardiovascular Medicine


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