The biological activity of atrial natriuretic factor cleaved by endoprotease 3.4.24.11

Autor:	G. Ghai, R. D. Ghai, J. L. Sonnenberg, Yumi Sakane, R. L. Webb
Rok vydání:	1991
Předmět:	Male Muscle Relaxation Natriuresis Receptors Cell Surface Biology In Vitro Techniques Cleavage (embryo) Biochemistry Muscle Smooth Vascular Atrial natriuretic peptide In vivo otorhinolaryngologic diseases Animals Aorta chemistry.chemical_classification Dose-Response Relationship Drug Biological activity Rats Inbred Strains Metabolism musculoskeletal system Peptide Fragments Diuresis Rats Enzyme chemistry embryonic structures cardiovascular system Adrenal Cortex Molecular Medicine Cattle Neprilysin Receptors Atrial Natriuretic Factor hormones hormone substitutes and hormone antagonists Atrial Natriuretic Factor
Zdroj:	Journal of enzyme inhibition. 4(3)
ISSN:	8755-5093
Popis:	Ring cleavage of atrial natriuretic peptide (ANF) between Cys7 and PheH by endoprotease 3.4.24.11 yields X-ANF. Since endoprotease 3.4.24.11 may contribute to ANF metabolism in vivo. the present study determined if X-ANF exhibits reduced biological activity in comparison to the parent molecule.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f7cff0a11ce6121419624edddd55754d https://pubmed.ncbi.nlm.nih.gov/1645400 Zobrazit plný text záznamu