Conversion of renin substrate tetradecapeptide to angiotensin II by rat MAB elastase-2 (2004)
- Authors:
- USP affiliated authors: SANTOS, CARLOS FERREIRA DOS - FOB ; SALGADO, MARIA CRISTINA DE OLIVEIRA - FMRP ; OLIVEIRA, EDUARDO BRANDT DE - FMRP
- Unidades: FOB; FMRP
- DOI: 10.1139/y04-102
- Assunto: ANGIOTENSINA II
- Language: Inglês
- Abstract: A new approach for the purification of rat mesenteric arterial bed IMAB) elauase-2 has been developed using the chromogenic substrates N-succinyl-AIa-AIa-Pro-Phe-p-nitroanilide and N-succinyl-Ala-Ala-Pro-Leu-p-nitroanilide to monitor the enzymatic activity during various stages of purification. The purified enzyme was evaluated in the presence of various inhibitors and confimed to have angiotensin (Ang) II -forming ability. The active site-directed inhibitor acetyl-Ala-Ala-Pro-Leu-chloromethyIketone (100'mü'mol.'L POT.-1'), described for human pancreatic elastase-2, abolished the enzymatic activity, confirming that the enzyme is an elastase-2. Chymostatin (100'mü'mol.'L POT.-1') an inhibitor regarded as selective for chymases, also showed a remarkable inhibitory effect (94%), whereas captopril (100'mü'mol.'L POT.-1') had no effect at all on the Ang II-forming activity. The Ang II precursor ronin substrate tetradecapeptide (RS-14P) was converted into Ang II by the rat MAB elastase-2 with the following kinetic constants: 'K IND.m' = 124 mais ou menos 21 'mü'mol.'L POT-1'; 'K IND.cat' = 629 'min POT.-1'; calalytic efficiency ('K IND.cat'/'K IND.m') = 5.1 'min POT.-1' 'mü''(mol/L) POT.-1' t. In conclusion, the strategy for the purification of rat MAB elastase-2 with the chromogenic substrates proved to be simple, rapid. accurate, and highly reproducible; there-fore, it can be reliably and conveniently used to routinely purify this enzyme.The kinetic parameters for the formation of Ang II from RS-14P by rat MAB elastase-2 emphasize differences in substrate specificity between this and other Ang II-forming enzymes
- Imprenta:
- Source:
- Título do periódico: Canadian Journal of Physiology and Pharmacology
- ISSN: 0008-4212
- Volume/Número/Paginação/Ano: v. 82, p. 1000-1005, 2004
- Este periódico é de assinatura
- Este artigo NÃO é de acesso aberto
- Cor do Acesso Aberto: closed
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ABNT
SANTOS, Carlos Ferreira dos et al. Conversion of renin substrate tetradecapeptide to angiotensin II by rat MAB elastase-2. Canadian Journal of Physiology and Pharmacology, v. 82, p. 1000-1005, 2004Tradução . . Disponível em: https://doi.org/10.1139/y04-102. Acesso em: 19 abr. 2024. -
APA
Santos, C. F. dos, Greene, A. S., Salgado, M. C. de O., & Oliveira, E. B. de. (2004). Conversion of renin substrate tetradecapeptide to angiotensin II by rat MAB elastase-2. Canadian Journal of Physiology and Pharmacology, 82, 1000-1005. doi:10.1139/y04-102 -
NLM
Santos CF dos, Greene AS, Salgado MC de O, Oliveira EB de. Conversion of renin substrate tetradecapeptide to angiotensin II by rat MAB elastase-2 [Internet]. Canadian Journal of Physiology and Pharmacology. 2004 ; 82 1000-1005.[citado 2024 abr. 19 ] Available from: https://doi.org/10.1139/y04-102 -
Vancouver
Santos CF dos, Greene AS, Salgado MC de O, Oliveira EB de. Conversion of renin substrate tetradecapeptide to angiotensin II by rat MAB elastase-2 [Internet]. Canadian Journal of Physiology and Pharmacology. 2004 ; 82 1000-1005.[citado 2024 abr. 19 ] Available from: https://doi.org/10.1139/y04-102 - Caracterização da elastase-2 de rato: uma enzima formadora de angiotensina II
- Functional role, cellular source, and tissue distribution of rat elastase-2, an angiotensin II-forming enzyme
- Potentiation of bradykinin effect by angiotensin-converting enzyme inhibition does not correlate with angiotensin-converting enzyme activity in the rat mesenteric arteries
- Angiotensin I metabolism: differences between the rat mesenteric bed and cardiac perfusates
- The early phase of pressure-overload cardiac hypertrophy is associated with an increased breakdown of bradykinin in the rat cardiac perfusate
- Angiotensin I metabolism in cardiac perfusate of aortic-banded rats
- Immobilized analogues of sunflower trypsin inhibitor-1 constitute a versatile group of affinity sorbents for selective isolation of serine proteases
- Characterization of a local renin-angiotensin system in rat gingival tissue
- Caracterização cinética e especificidade da elastase-2 conversora de angiotensina do perfusato do leito arterial mesentérico de rato
- Caracterização cinética e especificidade da elastase-2 conversora de angiotensina do perfusato do leito arterial mesentérico de rato
Informações sobre o DOI: 10.1139/y04-102 (Fonte: oaDOI API)
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