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

Autor:	Wolfgang Landgraf, Franz Hofmann, Michael Rack, H. H. Ruf
Rok vydání:	1987
Předmět:	chemistry.chemical_classification Enzyme chemistry Second messenger system Protein primary structure Biophysics Cooperative binding Protein kinase A cGMP-dependent protein kinase Fluorescence Dissociation (chemistry)
Zdroj:	Signal Transduction and Protein Phosphorylation ISBN: 9781475701685
DOI:	10.1007/978-1-4757-0166-1_13
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::34e3f0ddc24a2d50016a8b6e8e6048eb https://doi.org/10.1007/978-1-4757-0166-1_13 Zobrazit plný text záznamu