The Sites of Interaction of Calmodulin with Phosphofructokinase

  • Bärbel Buschmeier
  • Helmut E. Meyer
  • Hans-Hermann Kiltz
  • Ludwig M. G. HeilmeyerJr.
  • Georg W. Mayr
Conference paper
Part of the NATO ASI Series book series (NSSA, volume 135)


Calmodulin is a multifunctional calcium-binding protein found in all eukaryotic cells (for review see 1). It consists of four Ca++-binding helix-loop-helix domains which are homologous to each other and are often referred to as the EF-hand structures (2). Upon binding of calcium ions, calmodulin undergoes conformational changes (1,3–5) allowing it to interact with several target proteins.


Acetic Anhydride Basic Residue Myosin Light Chain Kinase Tryptic Fragment Dimeric Enzyme 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Bärbel Buschmeier
    • 1
  • Helmut E. Meyer
    • 1
  • Hans-Hermann Kiltz
    • 1
  • Ludwig M. G. HeilmeyerJr.
    • 1
  • Georg W. Mayr
    • 1
  1. 1.Inst. für Physiologische Chemie, Abt. für Biochemie Supramolekularer SystemeRuhr-UniversitätBochumGermany

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