Abstract: A modified uricase is described herein, as well as a method of reducing a level of uric acid by contacting a medium with the modified uricase. The modified uricase comprises a uricase polypeptide crosslinked by at least one bifunctional linking moiety that comprises a poly(alkylene glycol) moiety. A molecular weight of the bifunctional linking moiety is from about 1.5 kDa to about 4 kDa, and/or the modified uricase comprises a plurality of polypeptides having the amino acid sequence SEQ ID NO: 2. Further described is a polypeptide having the amino acid sequence SEQ ID NO: 2. A process of preparing the modified uricase is also described, comprising contacting the polypeptide with a crosslinking agent that comprises a poly(alkylene glycol) moiety and at least two aldehyde groups, to obtain a conjugate; and contacting the conjugate with a reducing agent.

Abstract: A modified DNase protein is described herein as well as pharmaceutical compositions comprising same, the modified DNase protein comprising a DNase polypeptide attached to at least two poly(alkylene glycol) moieties. Further described herein is a process of preparing a modified DNase protein, the process comprising: contacting the polypeptide with an agent that comprises a poly(alkylene glycol) attached to an aldehyde group, to obtain a conjugate of the polypeptide and the agent; and contacting the conjugate with a reducing agent.

Abstract: Modified DNase I protein in which one or more amino acids of a DNase I protein are modified non-cellularly, are provided. The modified DNase I protein exhibits a DNA hydrolytic activity in the presence of actin and an improved DNA hydrolytic activity compared to a homologous non-modified DNase I protein. Processes of preparing the modified DNase I protein and uses thereof in, for example, reducing a DNA content in sputum and/or in treating a disease or condition associated with excess extracellular DNA in a fluid, secretion or tissue of a subject, are also provided.

Abstract: Multimeric protein structures comprising at least two alpha-galactosidase monomers being covalently linked to one another via a linking moiety are disclosed herein, as well a process for preparing same, and methods of treating Fabry disease via administration of a multimeric protein structure. The disclosed multimeric protein structures exhibit an improved performance, in terms of enhanced activity and/or a longer lasting activity under both lysosomal conditions and in a serum environment.

Abstract: Modified DNase I protein in which one or more amino acids of a DNase I protein are modified non-cellularly, are provided. The modified DNase I protein exhibits a DNA hydrolytic activity in the presence of actin and an improved DNA hydrolytic activity compared to a homologous non-modified DNase I protein. Processes of preparing the modified DNase I protein and uses thereof in, for example, reducing a DNA content in sputum and/or in treating a disease or condition associated with excess extracellular DNA in a fluid, secretion or tissue of a subject, are also provided.

Abstract: Modified DNase I protein in which one or more amino acids of a DNase I protein are modified non-cellularly, are provided. The modified DNase I protein exhibits a DNA hydrolytic activity in the presence of actin and an improved DNA hydrolytic activity compared to a homologous non-modified DNase I protein. Processes of preparing the modified DNase I protein and uses thereof in, for example, reducing a DNA content in sputum and/or in treating a disease or condition associated with excess extracellular DNA in a fluid, secretion or tissue of a subject, are also provided.

Abstract: Multimeric protein structures comprising at least two alpha-galactosidase monomers being covalently linked to one another via a linking moiety are disclosed herein, as well a process for preparing same, and methods of treating Fabry disease via administration of a multimeric protein structure. The disclosed multimeric protein structures exhibit an improved performance, in terms of enhanced activity and/or a longer lasting activity under both lysosomal conditions and in a serum environment.

Abstract: Multimeric protein structures comprising at least two alpha-galactosidase monomers being covalently linked to one another via a linking moiety are disclosed herein, as well a process for preparing same, and methods of treating Fabry disease via administration of a multimeric protein structure. The disclosed multimeric protein structures exhibit an improved performance, in terms of enhanced activity and/or a longer lasting activity under both lysosomal conditions and in a serum environment.

Abstract: Multimeric protein structures comprising at least two alpha-galactosidase monomers being covalently linked to one another via a linking moiety are disclosed herein, as well a process for preparing same, and methods of treating Fabry disease via administration of a multimeric protein structure. The disclosed multimeric protein structures exhibit an improved performance, in terms of enhanced activity and/or a longer lasting activity under both lysosomal conditions and in a serum environment.

Abstract: Multimeric protein structures comprising at least two alpha-galactosidase monomers being covalently linked to one another via a linking moiety are disclosed herein, as well a process for preparing same, and methods of treating Fabry disease via administration of a multimeric protein structure. The disclosed multimeric protein structures exhibit an improved performance, in terms of enhanced activity and/or a longer lasting activity under both lysosomal conditions and in a serum environment.

Abstract: Modified DNase I protein in which one or more amino acids of a DNase I protein are modified non-cellularly, are provided. The modified DNase I protein exhibits a DNA hydrolytic activity in the presence of actin and an improved DNA hydrolytic activity compared to a homologous non-modified DNase I protein. Processes of preparing the modified DNase I protein and uses thereof in, for example, reducing a DNA content in sputum and/or in treating a disease or condition associated with excess extracellular DNA in a fluid, secretion or tissue of a subject, are also provided.

Abstract: Multimeric protein structures comprising at least two alpha-galactosidase monomers being covalently linked to one another via a linking moiety are disclosed herein, as well a process for preparing same, and methods of treating Fabry disease via administration of a multimeric protein structure. The disclosed multimeric protein structures exhibit an improved performance, in terms of enhanced activity and/or a longer lasting activity under both lysosomal conditions and in a serum environment.

Abstract: Multimeric protein structures comprising at least two alpha-galactosidase monomers being covalently linked to one another via a linking moiety are disclosed herein, as well a process for preparing same, and methods of treating Fabry disease via administration of a multimeric protein structure. The disclosed multimeric protein structures exhibit an improved performance, in terms of enhanced activity and/or a longer lasting activity under both lysosomal conditions and in a serum environment.

Abstract: Multimeric protein structures comprising at least two alpha-galactosidase monomers being covalently linked to one another via a linking moiety are disclosed herein, as well a process for preparing same, and methods of treating Fabry disease via administration of a multimeric protein structure. The disclosed multimeric protein structures exhibit an improved performance, in terms of enhanced activity and/or a longer lasting activity under both lysosomal conditions and in a serum environment.

Abstract: Conjugates of a saccharide and a biomolecule, covalently linked therebetween via a non-hydrophobic linker and methods of preparing same are disclosed. Also disclosed are medical uses utilizing such conjugates. Glycosylation reagents for use in preparing these conjugates are also disclosed. Glycosylated proteins, characterized by improved performance, are also disclosed.

Abstract: A method of treating or preventing Parkinson's disease in a subject in need thereof is disclosed. The method comprises administering to the subject a therapeutically effective amount of AChE-R, wherein the AChE-R is devoid of an N-terminal extension. An additional method of treating or preventing Parkinson's disease in a subject is disclosed. The method comprises administering to the subject a therapeutically effective amount of AChE-R, wherein the AChE-R comprises a modification for increasing bioavailability.

Abstract: Multimeric protein structures are disclosed herein, as well a process for preparing same, and methods employing same for treating various diseases or disorders. The multimeric protein structures comprise at least two monomers of a therapeutic protein, including a TNF-alpha, a luteinizing hormone, an immunoglobin, a TNF-alpha receptor, a CTLA-4, a urate oxidase, a VEGF, a PDGF, a VEGF receptor, a PDGF receptor, an interleukin-17, and/or fragments thereof, the monomers being covalently linked to one another via a linking moiety. The multimeric protein structures exhibit improved performance as compared to the corresponding native proteins, including a longer lasting activity in vivo.

Abstract: Multimeric protein structures comprising at least two glucocerebrosidase molecules being covalently linked to one another via a linking moiety are disclosed herein, as well a process for preparing same, and uses thereof in the treatment of Gaucher disease. The multimeric protein structures are characterized by longer-lasting activity as compared to native glucocerebrosidase both in serum and in lysosomes.

Abstract: Conjugates of a saccharide and a biomolecule, covalently linked therebetween via a non-hydrophobic linker and methods of preparing same are disclosed. Also disclosed are medical uses utilizing such conjugates. Glycosylation reagents for use in preparing these conjugates are also disclosed. Glycosylated proteins, characterized by improved performance, are also disclosed.