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Urodilatin (CDD/ANP‐95‐126) is not biologically inactivated by a peptidase from dog kidney cortex membranes in contrast to atrial natriuretic peptide/cardiodilatin (α‐hANP/CDD‐99‐126)
Author(s) -
Gagelmann Michael,
Hock Dieter,
Forssmann Wolf-Georg
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80436-8
Subject(s) - atrial natriuretic peptide , chemistry , proteolysis , membrane , peptide , kidney , cleavage (geology) , renal cortex , natriuretic peptide , biochemistry , medicine , endocrinology , enzyme , biology , paleontology , fracture (geology) , heart failure
Atrial natriuretic peptide (CDD/ANP‐99‐126) is rapidly inactivated by a membrane preparation from dog kidney cortex. Inactivation occurs by cleavage of the ring structure in the position between Cys‐105 and Phe‐106. A unique proteolytic product separated by HPLC on reverse‐phase column appears as a single peak which elutes prior the intact peptide. In contrast, CDD/ANP‐95‐126 (urodilatin) which is released from the kidney is not destroyed by proteolysis using an identical membrane preparation.

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