Analysis of lactase processing in rabbit

Mauro Rossi, Luigi Maiuri, Virginia M. Salvati, Concetta Russomanno, Salvatore Auricchio

Research output: Contribution to journalArticlepeer-review


The proteolytic processing of rabbit intestinal lactase-phlorizin-hydrolase (LPH) was studied by pulse-chase and continuous labeling experiments in organ culture from 15-day-old rabbits in the presence of glycosylation and processing inhibitors. Monensin and brefeldin A inhibited the two proteolytic cleavages of the precursor indicating that they are post-Golgi events as previously reported for the unique cleavage of LPH in man [1]. The inhibition was not related to a concomitant alteration glycosylation; in fact, if trimming was blocked by MDNM the abnormal glycosylated precursor was proteolytically processed normally. Finally the use of the anti-microtubular drug colchicine strongly inhibited both cleavages and caused accumulation of the complex-glycosylated precursor form in the brush border fraction indicating that proteolytic events depend on intact microtubule (transport).

Original languageEnglish
Pages (from-to)299-303
Number of pages5
JournalFEBS Letters
Issue number2
Publication statusPublished - Dec 27 1993


  • Biosynthesis
  • Lactase
  • Proteolysis inhibition
  • Rabbit
  • Suckling

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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