Some properties of spectrin-like proteins from Pisum sativum

Z Naturforsch C J Biosci. 1997 Mar-Apr;52(3-4):180-6. doi: 10.1515/znc-1997-3-408.

Abstract

Proteins cross-reacting with antibodies directed against alpha- and beta-spectrin were recently detected in plant cells. In this report we have studied the ability of these proteins to interact with other components of membrane skeleton such as ankyrin, f-actin and calmodulin. It was found that the polypeptide of high molecular weight reacting with anti-alpha-spectrin antibody binds calmodulin in Ca(2+)-dependent manner. Protein complexes containing polypeptides cross-reacting with anti-spectrin antibodies interact with muscle f-actin (in co-sedimentation assay) and with erythrocyte ankyrin (ELISA-type assay). These data further substantiate a possibility of occurrence of spectrin-based membrane skeleton in higher plant cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Animals
  • Ankyrins / metabolism
  • Antibodies
  • Calmodulin / metabolism
  • Cross Reactions
  • Enzyme-Linked Immunosorbent Assay
  • Erythrocytes / metabolism
  • Molecular Weight
  • Muscle, Skeletal / metabolism
  • Pisum sativum / chemistry*
  • Plant Proteins / chemistry*
  • Plant Proteins / isolation & purification
  • Plant Proteins / metabolism*
  • Rabbits
  • Spectrin / chemistry*
  • Spectrin / isolation & purification
  • Spectrin / metabolism

Substances

  • Actins
  • Ankyrins
  • Antibodies
  • Calmodulin
  • Plant Proteins
  • Spectrin