Ca2+-Dependent Mobility Shift of Parvalbumin in One- and Two-Dimensional Gel-Electrophoresis

  • H.-J. Gregersen
  • C. W. Heizmann
  • U. Kaegi
  • M. R. Celio
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 269)


Under Ca2+-loaded conditions parvalbumin migrates in one- and two-dimensional gel-systems as a double-band or -spot whereas in Ca2+-free condition it appears as one band or spot.

Parvalbumin (PV), a member of the family of calcium-binding proteins [1], was first described in 1934 [2] and occurs in fast-contracting muscles and in subpopulations of neurons in vertebrates and humans [3,4,5]. The physical characteristics of molecular weight (Mv 12 KD), isoelectric point (pI 4.9) and Ca2+ -binding properties are established (PV binds 2 Ca2+ per molecule) [5,6]. Physiological roles discussed for PV range from trigger- to buffer-protein of intracellular Ca2+-ions [7]. In this paper we report an as yet not described mobility shift of PV in gel-electrophoresis after manipulation of the Ca2+ concentration, which may have implications for its physiological function.


Free Condition Apparent Molecular Weight Dependent Mobility High Electrophoretic Mobility Dependent Conformational Change 
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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • H.-J. Gregersen
    • 1
  • C. W. Heizmann
    • 2
  • U. Kaegi
    • 2
  • M. R. Celio
    • 1
  1. 1.Institut für AnatomieChristian Albrechts Universität zu KielKielWest-Germany
  2. 2.Abtlg für Klin. ChemieUniversitäts-KinderklinikZürichSwitzerland

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