Abstract

The maturational decline in lactase-phlorizin hydrolase (LPH) activity was studied in groups of young rats ranging from suckling to early post-weaned states. Associated maturational increases in sucrase-isomaltase (SI) and maltase-glucoamylase (MG) activities were also examined as a comparison. Over this time period changes in cellular concentrations of the three enzymes were observed, reflecting corresponding changes in enzyme activities. Synthesis patterns accompanying these maturational changes in concentration were examined using labelled leucine as a marker. Synthesis of LPH was found to be maintained at constant rates independent of the maturation-associated decline in its concentration, whereas the increases in cellular concentrations of SI and MG were due to accelerated synthesis of the enzyme. Turnover of LPH, based on both the fractional synthesis rate and the disappearance rate of labelled leucine from prelabelled LPH pools, was increased in a quantitatively similar way to the decline in LPH concentration. These findings are consistent with our earlier proposal that the maturational decline of LPH occurs because of accelerated turnover, without a decrease in its rate of synthesis.

View details for Web of Science ID A1992HF96800015

View details for PubMedID 1540126