Results 231 to 240 of about 40,840 (280)
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Guanyl cyclase of Bacilluslicheniformis
Biochemical and Biophysical Research Communications, 1972Abstract Guanyl cyclase activity was detected in extracts of Bacillus licheniformis strain A-5. The enzyme is associated with the 105,000 × g particulate fraction of the extract, requires Mn++ for full activity, has a pH optimum of 8.5, and has an apparent Km for GTP of 5mM.
R.W. Bernlohr, V.L. Clark
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Guanylate Cyclase Activating Proteins, Guanylate Cyclase and Disease
2002A range of cone and cone-rod dystrophies (CORD) have been observed in man, caused by mutations in retinal guanylate cyclase 1 (RetGC1) and guanylate cyclase activating protein 1 (GCAP 1). The CORD causing mutations in RetGC1 are located at a mutation "hot spot" within the dimerisation domain, where R838 is the key residue.
Annette M. Payne +5 more
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Adenylate and Guanylate Cyclases in Tetrahymena [PDF]
, 1996 Cyclic nucleotides, such as cyclic AMP (cAMP) and cyclic GMP (cGMP), are of fundamental importance in regulating the many physiologic processes in a wide variety of living cells, acting as messengers interacting between receptor sites on the cell membrane and intracellular activity.
S. Umeki, Y. Nozawa
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Current Opinion in Structural Biology, 2006
Soluble guanylate cyclase (sGC) is a mammalian nitric oxide (NO) sensor. When NO binds to the sGC heme, its GTP cyclase activity markedly increases, thus generating cyclic GMP, which serves to regulate several cell signaling functions. A good deal is known about the kinetics and equilibrium of binding of NO to sGC, leading to a proposed multistep ...
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Soluble guanylate cyclase (sGC) is a mammalian nitric oxide (NO) sensor. When NO binds to the sGC heme, its GTP cyclase activity markedly increases, thus generating cyclic GMP, which serves to regulate several cell signaling functions. A good deal is known about the kinetics and equilibrium of binding of NO to sGC, leading to a proposed multistep ...
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Biochemistry of Soluble Guanylate Cyclase
2009Nitric oxide (NO) functions in biology as both a critical cytotoxic agent and an essential signaling molecule. The toxicity of the diatomic gas has long been accepted; however, it was not known to be a signaling molecule until it was identified as the endothelium-derived relaxing factor (EDRF). Since this discovery, the physiological signaling pathways
Emily R. Derbyshire, Michael A. Marletta
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Activation of guanyl cyclase and adenyl cyclase by secretin
Biochimica et Biophysica Acta (BBA) - Enzymology, 1973Abstract Properties of rat liver guanyl cyclase and adenyl cyclase and the effects of hormones on the activity of these enzymes have been investigated. 1. 1. Secretin ( 2·10 −7 –60·10 −7 M ) stimulates guanyl cyclase activity of 18 000 × g supernantants of rat liver homogenates with no change in the Michaelis-Menten constant
Sally A. Little +2 more
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Both soluble guanylate cyclase and particulate guanylate cyclase regulate myometrial contractility
American Journal of Obstetrics and Gynecology, 1998Our purpose was to compare the effects of agents stimulating particulate and soluble guanylate cyclase with spontaneous rat uterine contractions at midgestation and term.Uterine rings from midgestation (day 13) and term nonlaboring (day 22) rats were positioned in organ chambers for isometric force recording.
Robert E. Garfield +4 more
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Life Sciences, 1977
Guanylate cyclase from crude homogenates of vegetative Dictyosteliumdiscoideum has been characterized. It has a pH optimum of 8.0, temperature optimum of 25°C and requires 1 mM dithiothreitol for optimal activity. It strongly prefers Mn++ to Mg++ as divalent cation, requires Mn++ in excess of GTP for detectable activity, and is inhibited by high Mn ...
Annmarie Ward, Michael Brenner
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Guanylate cyclase from crude homogenates of vegetative Dictyosteliumdiscoideum has been characterized. It has a pH optimum of 8.0, temperature optimum of 25°C and requires 1 mM dithiothreitol for optimal activity. It strongly prefers Mn++ to Mg++ as divalent cation, requires Mn++ in excess of GTP for detectable activity, and is inhibited by high Mn ...
Annmarie Ward, Michael Brenner
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Emerging Therapeutic Targets, 2000
Soluble guanylate cyclase (sGC) is a heterodimeric haemoprotein, which represents the intracellular receptor for the ubiquitous biological messenger nitric oxide (NO). Activation of the enzyme facilitates conversion of GTP to the intracellular second messenger cGMP, and it is this molecule which mediates the majority of biological actions attributed to
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Soluble guanylate cyclase (sGC) is a heterodimeric haemoprotein, which represents the intracellular receptor for the ubiquitous biological messenger nitric oxide (NO). Activation of the enzyme facilitates conversion of GTP to the intracellular second messenger cGMP, and it is this molecule which mediates the majority of biological actions attributed to
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