Angiotensinogen cleavage by renin: importance of a structurally constrained N‐terminus

@article{StreatfeildJames1998AngiotensinogenCB,
  title={Angiotensinogen cleavage by renin: importance of a structurally constrained N‐terminus},
  author={R. M. Streatfeild-James and D. Williamson and R. Pike and D. Tewksbury and R. Carrell and P. Coughlin},
  journal={FEBS Letters},
  year={1998},
  volume={436}
}
  • R. M. Streatfeild-James, D. Williamson, +3 authors P. Coughlin
  • Published 1998
  • Chemistry, Medicine
  • FEBS Letters
  • 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 α1‐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… CONTINUE READING
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