Abstract: The present invention concerns the field of conjugated peptides suitable for the production of drugs having an improved plasma half-life. In particular the present invention relates to a conjugated protein, obtained by an enzymatic reaction via microbial transglutaminase (MTGase), and an improved process for removing residual transglutaminase from peptides or recombinant proteins enzymatically conjugated by microbial transglutaminase (MTGase) to hydrophilic non-immunogenic polymer at a glutamine side-chain through an amidic linkage, allowing to obtain purified conjugated peptides or proteins which are stable against the enzymatic hydrolysis of the amidic bond between the peptide or protein moiety and the hydrophilic polymer and being free from product derived degradation displays the stability required for a drug.

Abstract: The present invention relates to vesicles for topical delivery of drugs and cosmetics, named glyceromes and characterized by high content of glycerol. The invention further relates to pharmaceutical formulations and cosmetic products containing glycerosomes.

Abstract: The present invention is related to glucagon-like peptide-1 (GLP-1) and analogues insulinotropic peptides, monoconjugated to biocompatible polymeric molecules by enzymatic direct and site-specific transglutamination reaction as well as their pharmaceutical formulations and delivery systems for therapeutical application in dismetabolic pathologies such as type 2 diabetes.

Abstract: The present invention relates to vesicles for topical delivery of drugs and cosmetics, named glyceromes and characterized by high content of glycerol. The invention further relates to pharmaceutical formulations and cosmetic products containing glycerosomes.

Abstract: The present invention is related to glucagon-like peptide-1 (GLP-1) and analogues insulinotropic peptides, monoconjugated to biocompatible polymeric molecules by enzymatic direct and site-specific transglutamination reaction as well as their pharmaceutical formulations and delivery systems for therapeutical application in dismetabolic pathologies such as type 2 diabetes.

Abstract: Novel site-specific mono-conjugates of Granulocyte Colony Stimulating Factor (G-CSF) are hereby described, with analogues and derivatives thereof, which stimulate proliferation and differentiation of progenitor cells to mature neutrophiles. These conjugates have been obtained using transglutaminase to covalently and site-specifically bind a hydrophilic, non-immunogenic polymer to a single glutamine residue of the human G-CSF native sequence and analogues thereof. These novel site-specific mono-conjugated derivatives are recommended for therapeutic use since they are stable in solution and exhibit significant biological activity in vitro and a longer bloodstream half-life, as compared to the non-conjugated protein, with a consequent prolonged pharmacological activity.

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: Novel site-specific mono-conjugates of Granulocyte Colony Stimulating Factor (G-CSF) are hereby described, with analogues and derivatives thereof, which stimulate proliferation and differentiation of progenitor cells to mature neutrophiles. These conjugates have been obtained using transglutaminase to covalently and site-specifically bind a hydrophilic, non-immunogenic polymer to a single glutamine residue of the human G-CSF native sequence and analogues thereof. These novel site-specific mono-conjugated derivatives are recommended for therapeutic use since they are stable in solution and exhibit significant biological activity in vitro and a longer bloodstream half-life, as compared to the non-conjugated protein, with a consequent prolonged pharmacological activity.

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 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.

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.

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: A method is provided for producing non-glycosylated single chain prourokinase (proUK). The method comprises cultivating bacterial strains of E. coli which have been transformed with plasmids carrying the cDNA sequence coding for proUK.