Angiotensin I–Converting Enzyme Isoforms (High and Low Molecular Weight) in Urine of Premature and Full-Term Infants

摘要: Abstract —Angiotensin I–converting enzyme (ACE) isoforms in urine from healthy and mildly hypertensive untreated patients have been described the literature. Healthy subjects high- low-molecular-weight ACEs (170 65 kDa), whereas only (90 both of which resemble ACE N-terminal domain. Previous studies shown that is regulated during development, renal tubules premature human infants are not completely mature, given nephrogenesis complete until 36th week gestation. The aim present study was to purify characterize full-term detect presence N-domain form prenatal development. Urine concentrated an Amicon concentrator, dialyzed same equipment against 50 mmol/L Tris-HCl buffer (pH 8.0) contained 150 NaCl, submitted gel filtration on AcA-34 column equilibrated with above. Two peaks (P1 P2 for infants; TP1 TP2 infants) activity hippuryl-His-Leu ( K m , 3 mmol/L) were detected. All enzymes Cl − dependent inhibited by captopril EDTA. peptides angiotensin-(1-7) N -acetyl-Ser-Asp-Lys-Pro, as specific ACE, hydrolyzed TP2, suggests ACE. In infants, P1 12-fold lower than activity, but difference between 1.6-fold. Chromatography profiles analyzed days 1, 3, 7, 14, 21, 30 after birth. detected around 21st 30th days, day 1. These results suggest related development well full-length infants. This may indicate produce secrete even before term