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Gruber Véronique Berna Patrick P. Arnaud Thierry Bournat Philippe Clément Christèle Mison Dominique Olagnier Béatrice Philippe Laurence Theisen Manfred Baudino Sylvie Bénicourt Claude Cudrey Claire Bloës Carole Duchateau Nathalie Dufour Sylvie Gueguen Catherine Jacquet Séverine Ollivo Catherine Poncetta Christine Zorn Nathalie Ludevid Dolores Van Dorsselaer Alain Verger Robert Doherty Annette Mérot Bertrand Danzin Charles 《Molecular breeding : new strategies in plant improvement》2001,7(4):329-340
A recombinant dog gastric lipase with therapeutic potential for the treatment of exocrine pancreatic insufficiency was expressed in transgenic tobacco plants. We targeted the protein using two different signal sequences for either vacuolar retention or secretion. In both cases, an active glycosylated recombinant protein was obtained. The recombinant enzymes and the native enzyme displayed similar properties including acid resistance and acidic optimum pH. The proteolytic maturation and the specific activity of the recombinant proteins, however, were found to be dependent on subcellular compartmentalization. Expression levels of recombinant dog gastric lipase were about 5% and 7% of acid extractable plant proteins for vacuolar retention and secretion respectively. This expression system already has allowed the production of tens of grams of purified lipase through open-field culture of transgenic tobacco plants. 相似文献
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