Binding of Fluorescent Analogs of Cyclic GMP to cGMP-Dependent Protein Kinase
Conference paper
Abstract
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.
Keywords
Dissociation Kinetic Spectroscopic Signal Slow Dissociation Fast Dissociation Fluorescent Analog
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© Plenum Press, New York 1987