Calmodulin-like activity in the soluble fraction of Escherichia coli

Yasushi Iwasa, Kosei Yonemitsu, Kazuo Matsui, Kohji Fukunaga, Eishichi Miyamoto

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

A heat-stable factor with properties similar to those of calmodulin was found in the fraction containing Ca2+-dependent cyclic AMP phosphodiesterase of Escherichia coli. The factor activated such enzymes as cyclic nucleotide phosphodiesterase of bovine brain, (Ca2+,Mg2+)ATPase of human erythrocyte menbrane and myosin light chain kinase of rabbit myometrium in a Ca2+-dependent fashion with an apparent Ka of 5 × 10-5 M. The factor and brain calmodulin had no effect on the phosphodiesterase of E. coli. It may be concluded that calmodulin or a calmodulin-like protein occurs in prokaryotes.

Original languageEnglish
Pages (from-to)656-660
Number of pages5
JournalBiochemical and biophysical research communications
Volume98
Issue number3
DOIs
Publication statusPublished - 1981 Feb 12
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Calmodulin-like activity in the soluble fraction of Escherichia coli'. Together they form a unique fingerprint.

  • Cite this