Postnatal development of some membrane-bound enzymes of rat liver and kidney

1. The development of rat liver acyl-CoA:sn-glycerol-3-phosphate-O-acyl-transferase (EC 2.3.1.15) is characterized by an increase and decrease in activity during the neonatal period, followed by a second increase and decrease during the late weaning period. Kidney acyltransferase exhibits a similar peak in activity during the neonatal period before increasing to adult levels of activity during the late weaning period. 2. Nucleosidediphosphatase activity increases rapidly during the neonatal period and thereafter gradually rises to adult levels in both liver and kidney. The latency of the enzyme increases rapidly after birth and thereafter shows little change with age. The enzyme appears to be more latent in the liver than in the kidney at all ages studied. 3. NADPH-cytochrome c reductase of liver has a single steep maximum and minimum in activity during the neonatal period, before increasing again to adult levels during the late weaning period. The enzyme in kidney shows a similar developmental pattern but at much lower levels of specific activity. 4. sn-Glycerol-3-phosphate acyltransferase activity was significantly higher in rough than in smooth membranes throughout the neonatal period of rapid smooth membrane proliferation. This distribution of enzyme activity is unlike that reported by others in phenobarbital-induced smooth membrane proliferation and suggests a major role for rough membranes in phospholipid synthesis during the neonatal period. 5. The qualitative similarity in development in rough and smooth microsomal subfractions for each of these enzymes is in distinct contrast with results previously reported for glucose-6-phosphatase.