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- W2057840000 abstract "Incubation of rANP(5-28)--also called atriopeptin III (AP III)--with purified endopeptidase 24.11 led preferentially to the production of Phe-Arg-Tyr, while other products of minor importance were detected. One of these was identified as rANP(5-25) (atriopeptin I) (AP I). This hydrolysis pattern of endopeptidase 24.11 towards AP III differs from the known favored site of cleavage at the Cys7-Phe8 bond of rANP(1-28). Moreover, by comparison with rANP(1-28), the degradation rate of AP III was slower. These data suggest that N-terminal peptide truncation results in conformational and/or charge modifications leading to a different positioning of the peptide in the endopeptidase 24.11 active site. In most hypothalamic nuclei of the rat brain known to contain AP III and endopeptidase 24.11, the preferential Ser25-Phe26 bond hydrolysis, although supposed to be responsible for a reduced degradation rate, might represent an effective enzymatic pathway of catabolism for AP III." @default.
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- W2057840000 date "1993-03-01" @default.
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- W2057840000 title "Atriopeptin III degradation by endopeptidase 24.11: The Cys-Phe bond is not the preferential cleavage site" @default.
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- W2057840000 doi "https://doi.org/10.1016/0196-9781(93)90059-p" @default.
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