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- W2080522070 abstract "Aqueous extracts of rabbit liver are capable of hydrolyzing all the peptide bonds of [Asn1, Val5]-angiotensin II and [Asn1, Ile5]-angiotensin II. However, after dialysis against EDTA, these extracts degrade either form of angiotensin II primarily by the release of the C-terminal amino acid, phenylalanine. This carboxypeptidase is active at pH 7.4, stable at 56°, but inactivated at 100°. N-ethylmaleimide, 1 mM, reduces its activity 10%. The carboxypeptidase reacts slowly with N-Z-glycyl-l-phenylalanine and dose not hydrolyze N-α-carbo-β-naphthoxy-l-phenylalanine." @default.
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- W2080522070 date "1968-06-01" @default.
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- W2080522070 title "Degradation of angiotensin II by a carboxypeptidase of rabbit liver" @default.
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- W2080522070 doi "https://doi.org/10.1016/0005-2795(68)90087-1" @default.
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