Binding of Fluorescent Analogs of Cyclic GMP to cGMP-Dependent Protein Kinase

  • H. H. Ruf
  • M. Rack
  • W. Landgraf
  • F. Hofmann
Conference paper
Part of the NATO ASI Series book series (NSSA, volume 135)


Cyclic GMP (cGMP) is a second messenger for cellular regulation and activates cGMP-dependent protein kinase (cG-PK). cG-PK, a homo-dimer of 150 kDa, has four partially cooperative binding sites for cGMP with KD-values in the order of 10 to 200 nM as has been shown by binding studies with 3H-cGMP1,2. Two types of sites have been described, site 1 with high affinity and slow dissociation and site 2 with lower affinity and faster dissociation. The primary structure of the enzyme has been reported and assigned to functional domains3.


Dissociation Kinetic Spectroscopic Signal Slow Dissociation Fast Dissociation Fluorescent Analog 
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Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • H. H. Ruf
    • 1
  • M. Rack
    • 1
  • W. Landgraf
    • 1
  • F. Hofmann
    • 1
  1. 1.Physiologische ChemieUniversität des SaarlandesHomburg-SaarFed. Rep. Germany

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