Degradation of atrial natriuretic factor by kidney cortex membranes. Isolation and characterization of the primary proteolytic product.

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