SYNTHESIS OF HUMAN ANGIOTENSINOGEN (1-17) CONTAINING ONE OF THE PUTATIVE GLYCOSYLATION BINDING-SITES AND ITS HYDROLYSIS BY HUMAN RENIN AND PORCINE PEPSIN
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Data
1991-10-01
Autores
Hirata, Izaura Yoshico [UNIFESP]
Boschcov, Paulo [UNIFESP]
Oliveira, Maria Cecilia Ferraz de [UNIFESP]
Juliano, Maria Aparecida [UNIFESP]
Miranda, Antonio [UNIFESP]
Chagas, Jair Ribeiro [UNIFESP]
Tsuboi, Satoshi
Okada, Yoshio
Juliano, Luiz [UNIFESP]
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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.
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International Journal Of Peptide And Protein Research. Copenhagen: Munksgaard Int Publ Ltd, v. 38, n. 4, p. 298-307, 1991.