F. Gurdol et al., THE PRESENCE OF PROLIDASE ACTIVITY IN AMNIOTIC-FLUID AND ITS EVALUATION AS A MATURITY TEST, Biology of the neonate, 67(1), 1995, pp. 34-38
Prolidase (EC: 3.4.13.9) catalyses the hydrolysis of the peptide bond
involving the imino nitrogen of proline or hydroxyproline. Because of
the high proportion of imino acids in collagen, this enzyme plays an i
mportant role in its degradation. Since collagen turnover rate is expe
cted to be high during fetal growth, the level of prolidase activity m
ay reflect the degree of fetal maturation. In this study, amniotic flu
id prolidase I activity was measured in term and preterm pregnancies.
Lecithin concentration, which has been widely used for predicting feta
l lung maturity, was also measured. Prolidase I activity was positivel
y correlated with lecithin levels (n = 30; r = 0.42; p < 0.02), and al
so with birth weight of the babies (n = 30; r = 0.52; p < 0.01) in the
term-mature group. Dysmature babies had significantly lower prolidase
I activity in the amniotic fluid which was thought to be indicative o
f growth retardation.