Ankyrin inhibits binding of erythrocyte spectrin to phospholipid vesicles

Biochim Biophys Acta. 1994 Apr 20;1191(1):21-6. doi: 10.1016/0005-2736(94)90228-3.

Abstract

The studies on binding of erythrocyte spectrin to frozen and thawed phospholipid liposomes and its inhibition by ankyrin were performed. It was found that ankyrin inhibited up to 60% binding of spectrin by phosphatidylethanolamine/phosphatidylcholine vesicles. It was able to dissociate up to 40% of spectrin from this complex. Ankyrin inhibition of binding of phosphatidylserine/phosphatidylcholine vesicles by spectrin, although much lower, was also observed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Ankyrins / pharmacology*
  • Binding Sites
  • Cattle
  • Erythrocyte Membrane / metabolism
  • Liposomes / metabolism*
  • Phosphatidylcholines / metabolism
  • Phosphatidylethanolamines / metabolism
  • Phosphatidylserines / metabolism
  • Phospholipids / metabolism*
  • Spectrin / metabolism*

Substances

  • Ankyrins
  • Liposomes
  • Phosphatidylcholines
  • Phosphatidylethanolamines
  • Phosphatidylserines
  • Phospholipids
  • Spectrin