December 1, 1993Journal of Biological ChemistryOpen Access

Purification and characterization of a phosphoramidon-sensitive endothelin-converting enzyme in porcine aortic endothelium. OFF.

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Population

Porcine aortic endothelium (membrane fraction)

Design

Preclinical

Authors

KOKeizo OhnakaKyushu University RTR. TakayanagiCanon (Japan)MNM NishikawaKyushu University

Discussion

Member takes

Implication

Purified porcine ECE offers a biochemical reference; leaves open translation to human endothelin-targeted therapies.

Structured PICO

Population

Porcine aortic endothelium (membrane fraction)

Intervention

Purification and characterization of endothelin-converting enzyme

Outcome

Enzyme characteristics (pH optimum, inhibitors, kinetics, molecular mass)surrogate

The study successfully purified and characterized a phosphoramidon-sensitive endothelin-converting enzyme from porcine aortic endothelium, providing insights into its biochemical properties.

Cite This Study

Ohnaka et al. (1993) studied this question.

synapsesocial.com/papers/6a76ae68de5e3adfbdf6bf94 https://doi.org/10.1016/s0021-9258(19)74378-6

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Bookmark

Purification and characterization of a phosphoramidon-sensitive endothelin-converting enzyme in porcine aortic endothelium. OFF.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Purification and characterization of a phosphoramidon-sensitive endothelin-converting enzyme in porcine aortic endothelium. OFF.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider