| Title: | "Expression of a lipocalin in Pichia pastoris: secretion, purification and binding activity of a recombinant mouse major urinary protein" |
| Author(s): | Ferrari E; Lodi T; Sorbi RT; Tirindelli R; Cavaggioni A; Spisni A; |
| Address: | "Istituto di Chimica Biologica, Facolta di Medicina e Chirurgia, Universita degli Studi di Parma, Italy" |
| DOI: | 10.1016/s0014-5793(96)01436-6 |
| ISSN/ISBN: | 0014-5793 (Print) 0014-5793 (Linking) |
| Abstract: | "The proteins of the mouse major urinary protein complex (MUP), members of the lipocalin family, bind volatile pheromones and interact with the vomeronasal neuroepithelium of the olfactory system. We report the expression of a MUP protein using its native signal sequence for secretion in the methylotrophic yeast, Pichia pastoris. Mature recombinant MUP (rMUP) is secreted at a concentration of 270 mg/l in minimal medium and it is isolated from the culture supernatant by one step ion-exchange chromatography in a nearly pure form. Binding activity, tested with an odorant molecule which displays high affinity for native MUP, indicates that rMUP has a behavior similar to the native one. This finding suggests that the protein, and in particular its hydrophobic binding pocket, is properly folded" |
| Keywords: | "Alpha-Globulins/genetics/isolation & purification/*metabolism Amino Acid Sequence Animals Base Sequence Cloning, Molecular DNA, Complementary Genetic Vectors Mice Molecular Sequence Data Pichia/*genetics Proteins Recombinant Proteins/genetics/isolation &;" |
| Notes: | "MedlineFerrari, E Lodi, T Sorbi, R T Tirindelli, R Cavaggioni, A Spisni, A eng Research Support, Non-U.S. Gov't England 1997/01/13 FEBS Lett. 1997 Jan 13; 401(1):73-7. doi: 10.1016/s0014-5793(96)01436-6" |
