A comparative study of two structurally related analogs of Asp1-Ile5-angiotensin II
| Autor: | N. Ü. Gündoğan, R. K. Türker |
|---|---|
| Rok vydání: | 1974 |
| Předmět: |
medicine.medical_specialty
Sarcosine Colon Blood Pressure In Vitro Techniques Pharmacology Aminopeptidases Aminopeptidase chemistry.chemical_compound In vivo Internal medicine Adrenal Glands Endopeptidases medicine Animals Potency Isoleucine Aorta Aspartic Acid Chemistry Angiotensin II Isolated aorta Adrenalectomy Heart Valine General Medicine Rats Intestinal motility Perfusion Endocrinology Glycine Cats Rabbits Gastrointestinal Motility Half-Life Muscle Contraction |
| Zdroj: | Naunyn-Schmiedeberg's Archives of Pharmacology. 282:411-420 |
| ISSN: | 1432-1912 0028-1298 |
| DOI: | 10.1007/bf00500989 |
| Popis: | Two new synthetic analogs of Asp1-Ile5-angiotensin II, Sar1-Ile5-Ile8-angiotensin II and (N,N-dimethyl) Gly1-Ile5-Ile8-angiotensin II which are chemically related, have a potent competitive antagonistic action against Asp1-β-amid-Val5-angiotensin II on the rabbit isolated aorta, rat ascending colon, isolated perfused heart of cat and in vivo on the blood pressure and intestinal motility of the chloralose-anesthetized cat. Compared to Sar1-Ile5-Ile8-angiotensin II, (N,N-dimethyl) Gly1-Ile5-Ile8-angiotensin II has equal antagonistic potency on the isolated preparations but a lower potency in vivo. The duration of the antagonistic effect of (N,N-dimethyl) Gly1-Ile5-Ile8-angiotensin II in all preparations investigated has been found to be significantly shorter than that of Sar1-Ile5-Ile8-angiotensin II. It is assumed that replacement of sarcosine with N,N-dimethyl glycine at the NH2-terminal position, enhances the degradation of the analog by aminopeptidase and therefore decreases its half-life. |
| Databáze: | OpenAIRE |
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