Interaction Between Calmodulin and Target Proteins

  • Koichi Yagi
  • Michio Yazawa
  • Mitsuhiko Ikura
  • Kunio Hikichi
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 255)


When myosin light chain kinase (MLCK) activity was measured at various different free Ca2+ concentrations, the activity attained abruptively the maximum value within a very narrow concentration range of Ca2+. A result of this phenomenon is shown in Fig.1 (curve e), accompanied with the Ca2+ binding curve of calmodulin (curve a) (1). Since the Ca2+-calmodulin is known to work as an activator of MLCK, a large difference between the enzyme activation curve and the Ca2+ binding curve of calmodulin indicates that Ca2+ effect on the MLCK activity can not directly be explained by the comparison of these two curves. Olwin et al. have already shown that the affinity of Ca2+ to calmodulin was largely enhanced by the addition of MLCK (2). It is expected that the analysis of enhancing effect of MLCK to-the Ca2+ binding to calmodulin may give an answer how the enzyme attains the maximum activity within such a narrow concentration range of Ca2+ and how the Ca2+ concentration is fixed to this range. The Ca2+ binding to calmodulin was measured in the presence of mastoparan (curve c in Fig. 1) (3). Mastoparan is a small peptide composed of 14 amino acid residues, and Malencik and Anderson have reported a strong binding constant of mastoparan to calmodulin (4).


Myosin Light Chain Kinase Binding Curve Narrow Concentration Range Chicken Gizzard Myosin Light Chain Kinase Activity 


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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • Koichi Yagi
    • 1
  • Michio Yazawa
    • 1
  • Mitsuhiko Ikura
    • 2
  • Kunio Hikichi
    • 2
  1. 1.Department of Chemistry and High Resolution, Faculty of ScienceHokkaido UniversitySapporo 060Japan
  2. 2.NMR Laboratory, Faculty of ScienceHokkaido UniversitySapporo 060Japan

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