Abstract: The present invention relates to the expression and secretion in Saccharomyces cerevisiae of readily purifiable soluble variants of the Kex1 endopeptidase of Kluyveromyces lactis and the purification and use thereof for the in vitro processing of recombinant proteins usable in industrial applications. The soluble Kex1 endoproteases described here are free from the transmembrane domain of the native enzyme; the deletion of the transmembrane domain is achieved by removing at least 57 amino acid residues from the C-terminal.

Abstract: The present invention relates to the expression and secretion in Saccharomyces cerevisiae of readily purifiable soluble variants of the Kex1 endopeptidase of Kluyveromyces lactis and the purification and use thereof for the in vitro processing of recombinant proteins usable in industrial applications. The soluble Kex1 endoproteases described here are free from the transmembrane domain of the native enzyme; the deletion of the transmembrane domain is achieved by removing at least 57 amino acid residues from the C-terminal.

Abstract: The present invention relates to the expression and secretion in Saccharomyces cerevisiae of readily purifiable soluble variants of the Kex1 endopeptidase of Kluyveromyces lactis and the purification and use thereof for the in vitro processing of recombinant proteins usable in industrial applications. The soluble Kex1 endoproteases described here are free from the transmembrane domain of the native enzyme; the deletion of the transmembrane domain is achieved by removing at least 57 amino acid residues from the C-terminal.

Abstract: The present invention relates to the expression and secretion in Saccharomyces cerevisiae of readily purifiable soluble variants of the Kex1 endopeptidase of Kluyveromyces lactis and the purification and use thereof for the in vitro processing of recombinant proteins usable in industrial applications. The soluble Kex1 endoproteases described here are free from the transmembrane domain of the native enzyme; the deletion of the transmembrane domain is achieved by removing at least 57 amino acid residues from the C-terminal.

Abstract: The present invention describes a method for identifying compounds capable of preventing the aggregation of potentially amyloidogenic proteins. The invention encompasses (1) missing the protein of interest with the compound to be assayed (b) gradually increasing the temperature (c) detecting the appearance of amyloid fibres by turbidimetric measurements, and/or by visual inspection of the mixture, and/or by determining its protein content after spinning down the aggregated protein. Proteins that may be employed are polyglutaminated proteins containing a sequence of consecutive glutamines who length is suitable to promote heat-induced amyloid fibre formation. Preferably, the sequence length will be 32 reisudes or more; more preferably, the protein will be an ataxin-3 variant.

Abstract: The present invention relates to the expression and secretion in Saccharomyces cerevisiae of readily purifiable soluble variants of the Kex1 endopeptidase of Kluyveromyces lactis<and the purification and use thereof for the in vitro processing of recombinant proteins usable in industrial applications. The soluble Kex1 endoproteases described here are free from the trans-membrane domain of the native enzyme; the deletion of the transmembrane domain is achieved by removing at least 57 amino acid residues from the C-terminal.