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Cited by 3,284

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme.

Open access
Bredt, D S, Snyder, S H·1990·Proceedings of the National Academy of Sciences

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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Crossref · 10.1073/pnas.87.2.682

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Metadata

Authors
Bredt, D. S., & Snyder, S. H.
Venue
Proceedings of the National Academy of Sciences
Published
1990-01
Volume
87
Issue
2
Pages
682-685
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2059379142
Cited by
3,284
References
1
FWCI
97.89
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme. https://app.cochat.ai/papers/10.1073/pnas.87.2.682
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Bredt, D. S., & Snyder, S. H. (1990). Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.87.2.682

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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