Cap Z( 36 32) is a contaminant and the major inhibitor of actin neiwork formation in conventional actin preparations

James F. Casella, Donna J. Maack

Research output: Contribution to journalArticlepeer-review

Abstract

Previous studies have demonstrated that conventional actin preparations contain a potent factor which reduces the low shear viscosity of actin filaments (1). In this paper we demonstrate that Cap Z( 36 32), a recently described protein from skeletal muscle that caps the barbed end of actin filaments and localizes to the Z-line of skeletal muscle (2,3), is the major factor affecting the low shear viscosity of actin prepared from muscle as described by Spudich and Watt (4).

Original languageEnglish (US)
Pages (from-to)625-630
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume145
Issue number1
DOIs
StatePublished - May 29 1987

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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