In vitro biosynthesis of lactase in suckling and adult rabbits. Regulatory mechanisms involved in the decline of the lactase activity.
Steady state forms, levels and the in vitro biosynthesis of lactase-phlorizin hydrolase (LPH) proteins have been studied in proximal and middle intestine of suckling and adult rabbits. In most adult tissues the lactase activity and the LPH protein content were low and the synthesis rate of the 200 kDa lactase precursor was reduced in comparison to suckling tissues. In a few tissues with low enzymatic activity the LPH protein content was relatively high, and high lactase synthesis occurred. In addition, the ratio (labeled lactase)/(lactase protein) was lower in the middle jejunum of the adult rabbit than in the proximal region. Both decreased synthesis of LPH precursor and increased turnover or inactivation of the enzyme may cause the decline of the lactase activity.
Rossi
M
M
Department of Pediatrics, University Federico II of Naples, Italy.
Maiuri
L
L
Salvati
V M
VM
Russomanno
C
C
Capparelli
R
R
Auricchio
S
S
D000818:Animals; D000833:Animals, Suckling / Q000378:metabolism*; D004247:DNA / Q000378:metabolism; D007421:Intestine, Small / Q000201:enzymology* / Q000254:growth & development*; D007700:Kinetics; D010694:Lactase-Phlorizin Hydrolase / Q000096:biosynthesis*; D009924:Organ Culture Techniques; D011498:Protein Precursors / Q000096:biosynthesis; D011817:Rabbits; D001616:beta-Galactosidase / Q000096:biosynthesis*
D011498:Protein Precursors; D004247:DNA; D001616:beta-Galactosidase; D010694:Lactase-Phlorizin Hydrolase