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PMID:1689048
| Citation |
Bredt, DS and Snyder, SH (1990) Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme. Proc. Natl. Acad. Sci. U.S.A. 87:682-5 |
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| Abstract |
Nitric oxide mediates vascular relaxing effects of endothelial cells, cytotoxic actions of macrophages and neutrophils, and influences of excitatory amino acids on cerebellar cyclic GMP. Its enzymatic formation from arginine by a soluble enzyme associated with stoichiometric production of citrulline requires NADPH and Ca2+. We show that nitric oxide synthetase activity requires calmodulin. Utilizing a 2',5'-ADP affinity column eluted with NADPH, we have purified nitric oxide synthetase 6000-fold to homogeneity from rat cerebellum. The purified enzyme migrates as a single 150-kDa band on SDS/PAGE, and the native enzyme appears to be a monomer. |
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| Keywords |
Animals; Calcium/pharmacology; Calmodulin/antagonists & inhibitors; Calmodulin/metabolism; Cerebellum/enzymology; Chromatography, Affinity; Chromatography, DEAE-Cellulose; Edetic Acid/pharmacology; Enzymes/isolation & purification; Enzymes/metabolism; Kinetics; Molecular Weight; NADP/metabolism; Nitric Oxide Synthase; Rats; Sulfonamides/pharmacology; Trifluoperazine/pharmacology |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004517: nitric-oxide synthase activity |
ECO:0000314: |
F |
figure 3 |
complete | ||||
|
enables |
GO:0004517: nitric-oxide synthase activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
See also
References
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