Abstract: The present invention relates to a method for inducing the immune response of an individual against B-lymphoproliferative disorders. The method is based on DNA vaccination with the short peptide encompassing the CDR3 hypervariable region of immunoglobulin heavy chain (VH-CDR3) alone or in combination with at least another immunomodulating sequence.

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: Novel, genetically modified mammalian cell lines are described, which can produce glycoconjugates the oligosaccharide portions of which are more similar to the human one than those of the same glycoconjugates produced by cells which have not been genetically modified. The lines in question can be used for the production of recombinant glycoconjugates which are of therapeutic interest, in particular for the production of glycoproteins for use in human therapy, since the glycoconjugates produced in these modified lines have a lower immunogenic potential for man than corresponding glycoconjugates produced in cells which have not been genetically modified.

Abstract: The subject of the present invention is the construction of multicistronic eukaryotic plasmid expression vectors in which it is possible to express from two to four genes simultaneously and which are characterized by differently regulated bicistronic transcription units. The distinctive characteristic of these vectors is the presence of a CAP-independent translation initiation mechanism which is based on the ability of an IRES (internal ribosomal entry site) sequence to translate two proteins under the control of a single promoter. This family of multicistronic vectors can advantageously be used in various biotechnological applications in whcih the simultaneous expression of two or more genes is necessary, such as gene transfer protocols, DNA-immunization, or for the expression of different molecules in the same cell.

Abstract: Novel strains of genetically modified prokaryotic micro-organisms capable of expressing polypeptides having the enzyme activity of the enzymes uridine phosphorylase (UdP) and purine nucleoside phosphorylase (PNP) are described; the strains in question can be used, both in the form of whole cells and in the form of crude or purified extracts, to catalyse transglycosylation reactions between a donor nucleoside and an acceptor base with particularly high yields. The associated plasmid vectors are also described.

Abstract: Strains of genetically modified prokaryotic micro-organisms capable of expressing polypeptides having the enzyme activity of the enzymes uridine posphorylase (UdP) and purine nucleoside phosphorylase (PNP) are described; the strains in question can be used, both in the form of whole cells and in the form of crude or purified extracts, to catalyse transglycosylation reactions between a donor nucleoside and an acceptor base with particularly high yields. The associated plasmid vectors are also described.

Abstract: The preparation of novel biocatalysts is described; the biocatalysts are produced by the co-immobilization of the recombinant enzymes uridine phosphorylase and purine nucleoside phosphorylase by means of covalent bonds on solid substrates functionalized with epoxy groups. The novel biocatalysts are usable for successive reaction cycles, are resistant to heat and to the presence of solvents, and can advantageously be used in the industrial production of natural nucleosides and of modified analogues of pharmaceutical interest.