Fate of bradykinin-potentiating peptide 9a after intravenous injection.
The fat of less than Glu1-3H-labelled bradykinin-potentiating peptide 9a [BPP9a; less than Glu-Trp-Pro-Arg-Pro-Gln-Ile-Pro-Pro, an inhibitor of angiotensin-converting enzyme (peptidyl dipeptidase)] was studied in the rabbit. After intravenous injection, BPP9a was rapidly removed from blood and much of the associated radioactivity was excreted in urine. Approx. 8% of the radioactivity in urine collected 2h after drug administration occurred in the form of BPP9a itself, the remainder occurring in three lower homologues: less than Glu-Trp (60%), less Glu-Trp-Pro-Arg-Pro-Gln (20%) and less than Glu-Trp-Pro-Arg-Pro-Gln-Ile (12%). Hydrolysis was not accounted for by enzymes in blood or urine. Apparently hydrolysis occurred within the kidney, as less than Gl-Trp was obtained in 60% yield in urine of isolated rat kidney perfused with [less than Glu1-3H]BPP9a.
D000818:Animals; D005260:Female; D006868:Hydrolysis; D007275:Injections, Intravenous; D007668:Kidney / Q000378:metabolism; D009842:Oligopeptides / Q000378:metabolism*; D011817:Rabbits; D013722:Teprotide / Q000031:analogs & derivatives / Q000378:metabolism* / Q000652:urine
D009842:Oligopeptides; D013722:Teprotide