Abstract
The glutathione S-transferases (GST) are a group of enzymes present in a number of tissues, including liver and RBC's. They initiate detoxification of endogenous and exogenous substances by conjugation with glutathione, and might act as storage proteins by binding nonsubstrate compounds such as heme and bilirubin. They also exhibit non-selenium-dependent glutathione peroxidase (GSH-Px) activity. The low activity of Se-dependent GSH-Px in neonatal RBC's compared with those from adults, and comparatively high activity of RBC GST in fullterm (FT) neonates, prompted a study of developmental patterns of RBC GST in preterm (P) infants. RBC GST was assayed in 23 P infants (birth wt 700–2100gm) and 12 FT infants soon after birth. Results: P had significantly higher activity than FT (*p<.01). Within the P group, a highly significant negative correlation was found between birth wt and enzyme activity (r=−0.61; p<.01). We speculate that these developmental patterns might reflect changes in heme &/or bilirubin ligand functions associated with heme turnover rates. They might also indicate a physiological inverse relationship between Se-dependent and Se-independent GSH-Px activity during development, and might require a re-evaluation of the interaction of fetal anti-oxidant protective mechanisms.
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