In vitro biosynthesis of lactase in preweaning and adult rabbit

Mauro Rossi, Luigi Maiuri, Concetta Russomanno, Salvatore Auricchio

Research output: Contribution to journalArticlepeer-review


Lactase is synthesized is a high-mannose large precursor (200 kDa) which is subsequently complex-glycosylated (215 kDa) and split into the 150 kDa mature form. The regulatory mechanisms responsible for the decline of activity at weaning are not yet known. We have set up in vitro cultures of intestinal mucosa from suckling and adult rabbit and found that suckling and adult animals synthesize the same four forms of lactase-phlorizin hydrolase (LPH) but with a different distribution. In the proximal adult small intestine there is very little 180 kDa form, which is most probably a product of the 215 kDa complex-glycosylated precursor. The 180 kDa form comprises a greater percentage of total LPH in the middle of the small intestine in adult and particularly in sukling rabbits. In the latter tissue this form is apparently more stable than in the adult tissue. Posttranscriptional control of lactase synthesis is therefore different in the various parts of the adult small intestine, and it is different in the suckling as compared to adult tissue.

Original languageEnglish
Pages (from-to)260-264
Number of pages5
JournalFEBS Letters
Issue number3
Publication statusPublished - Nov 30 1992


  • Adult (rabbit)
  • Lactase-phlorizin hydrolase biosynthesis
  • Lactase-phlorizin hydrolase processing
  • Preweaning (rabbit)

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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