Abstract
RENIN is said to split a leucyl–leucine bond in alpha 2 globulin substrate—angiotensinogen—to yield a decapeptide, angiotensin I. Angiotensin I is subsequently converted into an octapeptide, angiotensin II, by a converting enzyme contained in plasma. Angiotensin II has a pressor activity. We have studied the effects of synthetic peptides with a leucyl–leucine bond and their derivatives on the activity of renin in the formation of angiotensin. The peptides were di-, tri-, tetra- and pentapeptides with leucyl–leucine bonds at the C-terminal end, in the middle position, at the N-terminal end or with one of the other structures as shown in Table 1.
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References
Haas, E., Lamfrom, H., and Goldblatt, H., Arch. Biochem. Biophys., 48, 256 (1954).
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KOKUBU, T., UEDA, E., FUJIMOTO, S. et al. Peptide Inhibitors of the Renin–Angiotensin System. Nature 217, 456–457 (1968). https://doi.org/10.1038/217456a0
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DOI: https://doi.org/10.1038/217456a0
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