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- W1495480944 abstract "Synthetic rat atrial natriuretic factor (r-ANF, 1-28) was incubated with rat kidney cortex membranes, and a predominant degradation product was identified by reverse-phase high performance liquid chromatography. The degradation product was subjected to amino acid analyses and found to have a composition identical to r-ANF. Amino-terminal sequence analyses identified two distinct amino-terminal residues and suggested that cleavage had occurred between the cysteine-phenylalanine bond (residues 7 and 8) of r-ANF. This degradative process could be inhibited by 1,10-phenanthroline and EDTA, suggesting that the enzyme responsible for proteolysis is a metalloendoprotease. The enzyme exhibits a Michaelis-Menten constant of approximately 10 microM for the metabolism of r-ANF and has a broad pH optimum between 8.5 and 9.5. These findings suggest that ANF may be initially degraded in the kidney at a single cleavage site within the 17-residue ring structure." @default.
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- W1495480944 date "1987-08-01" @default.
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- W1495480944 title "Degradation of atrial natriuretic factor by kidney cortex membranes. Isolation and characterization of the primary proteolytic product." @default.
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- W1495480944 doi "https://doi.org/10.1016/s0021-9258(18)60854-3" @default.
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