Binding of spectrin to hereditary spherocyte membranes

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

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

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
Volume14
Issue numberSUPPL. 3
DOIs
StatePublished - Jan 1 1982
Externally publishedYes

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Spherocytes
Spectrin
Membranes
Hereditary Spherocytosis
Proteins
Cell Shape
Erythrocyte Membrane
Skeleton
Osmolar Concentration
Binding Sites

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cardiology and Cardiovascular Medicine

Cite this

Binding of spectrin to hereditary spherocyte membranes. / Goodman, Steven; Weidner, Scott A.; Eyster, M. Elaine; Kesselring, Joseph J.

In: Journal of Molecular and Cellular Cardiology, Vol. 14, No. SUPPL. 3, 01.01.1982, p. 91-97.

Research output: Contribution to journalArticle

Goodman, Steven ; Weidner, Scott A. ; Eyster, M. Elaine ; Kesselring, Joseph J. / Binding of spectrin to hereditary spherocyte membranes. In: Journal of Molecular and Cellular Cardiology. 1982 ; Vol. 14, No. SUPPL. 3. pp. 91-97.
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