SYNTHESIS OF HUMAN ANGIOTENSINOGEN (1-17) CONTAINING ONE OF THE PUTATIVE GLYCOSYLATION BINDING-SITES AND ITS HYDROLYSIS BY HUMAN RENIN AND PORCINE PEPSIN

SYNTHESIS OF HUMAN ANGIOTENSINOGEN (1-17) CONTAINING ONE OF THE PUTATIVE GLYCOSYLATION BINDING-SITES AND ITS HYDROLYSIS BY HUMAN RENIN AND PORCINE PEPSIN

Author Hirata, Izaura Yoshico Autor UNIFESP Google Scholar
Boschcov, Paulo Autor UNIFESP Google Scholar
Oliveira, Maria Cecilia Ferraz de Autor UNIFESP Google Scholar
Juliano, Maria Aparecida Autor UNIFESP Google Scholar
Miranda, Antonio Autor UNIFESP Google Scholar
Chagas, Jair Ribeiro Autor UNIFESP Google Scholar
Tsuboi, Satoshi Google Scholar
Okada, Yoshio Google Scholar
Juliano, Luiz Autor UNIFESP Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
KOBE GAKUIN UNIV
Abstract The N-terminal heptadecapeptide of human angiotensinogen (Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Asn-Glu-Ser-Thr-NH2), with the C-terminal carboxyl group amidated, was synthesized in order to study the role of Asn-Glu-Ser, a putative carbohydrate binding site, on the hydrolysis by human renin. The synthesis was performed by fragment condensation using the Honzl and Rudinger azide procedure. In our conditions for azide segment condensation, histidine racemization was demonstrated to be negligible for most of the condensation reactions. Human renin liberates angiotensin I from h-angiotensinogen (1-17)-NH2 with a K(m) value of 3.4 x 10(-5) M, at pH 7.3 and 37-degrees being similar to h-angiotensinogen (1-13), an analog without the carbohydrate binding site. However, the V(max) value of 4.1 x 10(-9) mol/G.U. min is one order of magnitude higher. Porcine pepsin was demonstrated to cleave preferentially Leu10-Val11 bond and, surprisingly, His9-Leu10 as well.
Keywords ANGIOTENSINOGEN
GLYCOSYLATION
HUMAN RENIN
PEPTIDE SYNTHESIS
PORCINE PEPSIN
SUBSTRATE
Language English
Date 1991-10-01
Published in International Journal Of Peptide And Protein Research. Copenhagen: Munksgaard Int Publ Ltd, v. 38, n. 4, p. 298-307, 1991.
ISSN 0367-8377 (Sherpa/Romeo, impact factor)
Publisher Munksgaard Int Publ Ltd
Extent 298-307
Origin http://doi.org/10.1111/j.1399-3011.1991.tb01508.x
Access rights Closed access
Type Article
Web of Science ID WOS:A1991GL47600002
URI http://repositorio.unifesp.br/11600/44095

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