Stimulation of guanylate cyclase by EDTA and other chelating agents
| Autor: | Susan E. Nicol, V. B. Tuason, Susan E. Senogles, William H. Frey |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
GUCY1B3
GTP' Dopamine In Vitro Techniques Medicinal chemistry Divalent chemistry.chemical_compound Humans Magnesium Chelation Edetic Acid Chelating Agents chemistry.chemical_classification Manganese Activator (genetics) Guanylate cyclase activity GUCY1A3 General Medicine Enzyme Activation Kinetics EGTA chemistry Biochemistry Guanylate Cyclase Guanosine Triphosphate Caudate Nucleus |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Enzymology. 658:369-376 |
| ISSN: | 0005-2744 |
| DOI: | 10.1016/0005-2744(81)90307-7 |
| Popis: | The partially purified soluble guanylate cyclase (GTP pyrophosphatelyase(cyclizing), EC 4.6.1.2) from human caudate nucleus is stimulated from 2 to 4-fold by metal chelating agents. EDTA ( K 1 2 = 4.8 μ M is more potent than CDTA ( K 1 2 = 13.2 μ M ) or EGTA ( K 1 2 = 21.8 μ M ) at stimulating activity. Stimulation by chelating agents is apparently not due to removal of inhibitory divalent cations which contaminate the enzyme or reaction mixture. EDTA increases guanylate cyclase activity in part by increasing the affinity of the enzyme for the substrate (MgGTP) 10-fold. Dopamine inhibits partially purified guanylate cyclase in the presence or absence of EDTA. Dopamine increases the Ka of guanylate cyclase for the activator, free Mn2+, more than 50-fold, from 3 to 150 μM. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|