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Cited by 980

The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.

Purification and characterization of particulate endothelium-derived relaxing factor synthase from cultured and native bovine aortic endothelial cells.

Open access
Pollock, J S, Förstermann, U, Mitchell, J A, Warner, T D, Schmidt, H H, Nakane, M, Murad, F·1991·Proceedings of the National Academy of Sciences

Abstract

The particulate enzyme responsible for the synthesis of endothelium-derived relaxing factor has been purified from cultured and native (noncultured) bovine aortic endothelial cells. Purification of the solubilized particulate enzyme preparation by affinity chromatography on adenosine 2',5'-bisphosphate coupled to Sepharose followed by Superose 6 gel filtration chromatography resulted in a single protein band after denaturing polyacrylamide gel electrophoresis that corresponded to approximately 135 kDa. The enzyme activity in the various fractions was assayed by its stimulatory effect on soluble guanylyl cyclase of rat fetal lung fibroblasts (RFL-6 cells), by the formation of L-citrulline from L-arginine, by measuring nitrite/nitrate formation, and by bioassay on endothelium-denuded vascular strips. Endothelium-derived relaxing factor synthase was purified 3419-fold from the crude particulate fraction of cultured bovine aortic endothelial cells with a 12% recovery (RFL-6 assay). Purified endothelium-derived relaxing factor synthase required L-arginine, NADPH, Ca2+, calmodulin, and 5,6,7,8-tetrahydrobiopterin for full activity.

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Metadata

Authors
Pollock, J. S., Förstermann, U., Mitchell, J. A., Warner, T. D., Schmidt, H. H., Nakane, M., & Murad, F.
Venue
Proceedings of the National Academy of Sciences
Published
1991-12
Volume
88
Issue
23
Pages
10480-10484
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2042782418
Cited by
980
References
6
FWCI
27.61
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Purification and characterization of particulate endothelium-derived relaxing factor synthase from cultured and native bovine aortic endothelial cells. https://app.cochat.ai/papers/10.1073/pnas.88.23.10480
The paper
Pollock, J. S., Förstermann, U., Mitchell, J. A., Warner, T. D., Schmidt, H. H., Nakane, M., & Murad, F. (1991). Purification and characterization of particulate endothelium-derived relaxing factor synthase from cultured and native bovine aortic endothelial cells. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.88.23.10480

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

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.