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- W2000860631 abstract "Angiotensinogen, a plasma serpin, functions as a donor of the decapeptide angiotensin I, which is cleaved from the N‐terminus by renin. To assess the contribution of the serpin framework to peptide cleavage we produced a chimaeric molecule of α 1 ‐antitrypsin carrying the angiotensinogen N‐terminus and determined the kinetic parameters for angiotensin I release. The K m for plasma angiotensinogen was 18‐fold lower than for the chimaeric protein while the catalytic efficiency was four‐fold higher. We also show that Cys‐18 participates in a disulphide bond and propose that constraints on the N‐terminus profoundly affect the interaction with renin." @default.
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- W2000860631 date "1998-10-02" @default.
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- W2000860631 title "Angiotensinogen cleavage by renin: importance of a structurally constrained N-terminus" @default.
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- W2000860631 doi "https://doi.org/10.1016/s0014-5793(98)01145-4" @default.
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