Abstract: A production method of recombinant adeno-associated virus particles (rAAV virions) having less empty viral contamination is disclosed. The production method includes: (a) culturing mammalian cells containing an introduced AAV vector in a medium to release rAAV virions into the medium; (b) recovering a culture supernatant from the medium; and (c) purifying the rAAV virions from the recovered culture supernatant by affinity column chromatography using a material having an affinity for an AAV capsid protein as a stationary phase and anion column chromatography.

Abstract: Disclosed is a method for producing a fusion protein of human serum albumin and human growth hormone. The method comprises (a) a step of culturing a mammalian cell capable of producing the protein in a serum-free medium and causing the protein to be secreted into the culture fluid, (b) a step of collecting a culture supernatant by removing the mammalian cell from the culture fluid, and (c) a step of purifying the protein from the culture supernatant by using column chromatography using a material to which an antibody having an affinity for the protein is bound as a stationary phase, column chromatography using a material having an affinity for phosphate group as a stationary phase, cation exchange column chromatography, and size exclusion column chromatography.

Abstract: Disclosed is a fusion protein containing a brain-derived neurotrophic factor (BDNF). The fusion protein is a fusion protein of BDNF and a specific range of human anti-transferrin receptor antibody, which makes BDNF administered into the blood able to pass through the blood-brain barrier.

Abstract: A chromatography column for the use of separation of acidic sugar chains, wherein the column comprises a first column and a second column, the second column connected by a flow path downstream of an outlet of the first column, and selected from the following (1) or (2): (1) the carrier of the first column is hydrophobically modified silica having a group containing a primary amine, a secondary amine or/and a tertiary amine, and the carrier of the second column is a resin having a group containing a primary amine, a secondary amine or/and a tertiary amine; (2) the carrier of the first column is a resin having a group containing a primary amine, a secondary amine or/and a tertiary amine, and the carrier of the second column is hydrophobically modified silica having a group containing a primary amine, a secondary amine, or/and a tertiary amine.

Abstract: Aqueous pharmaceutical compositions containing a fusion protein of an antibody and a lysosomal enzyme as an active ingredient, which are stable enough to be marketed, are disclosed. The aqueous pharmaceutical composition, for example, comprises the fusion protein of the antibody and the lysosomal enzyme at a concentration of 0.5 to 20 mg/mL, sodium chloride at a concentration of 0.3 to 1.2 mg/mL, sucrose at a concentration of 50 to 100 mg/mL, a nonionic surfactant at a concentration of 0.15 to 3 mg/mL, a buffer at a concentration of 3 to 30 mM, and is adjusted to pH 5.0 to 7.5.

Abstract: The invention provides a nucleic acid molecule comprising a gene encoding a fusion protein of a ligand and a protein having physiological activity, to be used for expressing the fusion protein in cells, tissue or the body. The invention further provides a nucleic acid molecule comprising the fusion protein-encoding gene, which is in the form of a plasmid, in a form encapsulated in a recombinant virus virion, or a form encapsulated in liposomes or lipid nanoparticles. The invention further relates to the use of a medicine which is a nucleic acid molecule comprising the fusion protein-encoding gene.

Abstract: The present invention relates to a mutant of human ?-N-acetylglucosaminidase (hNAGLU), more specifically a hNAGLU mutant produced by adding a mutation to an amino acid sequence for hNAGLU such that an expression level of hNAGLU in a host cell in which a gene encoding hNAGLU is introduced can be increased compared with the case where a gene encoding wild-type hNAGLU is introduced. For example, the hNAGLU mutant has an amino acid sequence represented by SEQ ID NO: 3, SEQ ID NO: 5, SEQ ID NO: 9, SEQ ID NO: 11, SEQ ID NO: 15, or SEQ ID NO: 19, or has an amino acid sequence introduced a mutation to the amino acid sequence of any one of the hNAGLU mutants.

Abstract: An aqueous preparation containing a protein as an active ingredient which is stable in storage in solution and makes an injection pain reduced is provided. More specifically an aqueous preparation containing a phosphate buffer at a concentration of 1 to 20 mM and a protein as an active ingredient is provided. Further more specifically provided is an aqueous preparation containing a phosphate buffer at a concentration of 1 to 20 mM, human growth hormone as an active ingredient, a poloxamer as a non-ionic surfactant; and phenol as a isotonic agent.

Abstract: A chromatography column for the use of separation of acidic sugar chains, wherein the column comprises a first column and a second column, the second column connected by a flow path downstream of an outlet of the first column, and selected from the following (1) or (2): (1) the carrier of the first column is hydrophobically modified silica having a group containing a primary amine, a secondary amine or/and a tertiary amine, and the carrier of the second column is a resin having a group containing a primary amine, a secondary amine or/and a tertiary amine; (2) the carrier of the first column is a resin having a group containing a primary amine, a secondary amine or/and a tertiary amine, and the carrier of the second column is hydrophobically modified silica having a group containing a primary amine, a secondary amine, or/and a tertiary amine.

Abstract: An aqueous preparation containing a protein as an active ingredient which is stable in storage in solution and makes an injection pain reduced is provided. More specifically an aqueous preparation containing a phosphate buffer at a concentration of 1 to 20 mM and a protein as an active ingredient is provided. Further more specifically provided is an aqueous preparation containing a phosphate buffer at a concentration of 1 to 20 mM, human growth hormone as an active ingredient, a poloxamer as a non-ionic surfactant; and phenol as a isotonic agent.

Abstract: To provide a peptide, etc., capable of passing through the blood-brain barrier (BBB) by binding to a human transferrin receptor (hTfR). A peptide, etc., having the amino acid sequence shown in SEQ ID NO: 1 (Ala-Val-Phe-Val-Trp-Asn-Tyr-Tyr-Ile-Ile-Ser-Cys) or an amino acid sequence having substitutions, deletions, additions, and/or insertions of 1 to 10 amino acid residues (inclusive) in the amino acid sequence shown in SEQ ID NO: 1.

Abstract: Disclosed is a method for producing a glycoprotein using mammalian cells, wherein all or part of the non-reducing ends of N-glycoside binding sugar chains are mannose residues. The method is a method for producing glycoproteins using transformant mammalian cells which are prepared by introducing thereinto a ?-N-acetylglucosaminidase gene and inducing its expression.

Abstract: Disclosed are a human serum albumin mutant that can be linked to a physiologically active protein to increase the stability of the protein in the blood, as well as a resulting protein produced by linking with the mutant. The protein produced by linking with the mutant consists of a human serum albumin mutant comprising the amino acid sequence set forth as SEQ ID NO:3 or an amino acid sequence that, in comparison with it, lacks not more than 10 amino acid residues and/or has not more than 10 amino acid residues replaced, with the proviso that the asparagine residue occurring at position 318 and the threonine at position 320 from the N-terminus of the amino acid sequence set forth as SEQ ID NO:3 are preserved and linked by peptide bonds via a single amino acid residue (X) except proline placed between those two amino acid residues, and a physiologically active protein linked to the mutant.

Abstract: [Problem to be solved] To provide a therapeutic compound for neuronal ceroid lipofuscinosis. [Solution] Provided is a compound for treatment and/or prevention of neuronal ceroid lipofuscinosis represented by the following general formula [I]. In the general formula [I], R1 is a methyl group or a hydroxymethyl group, R2 is a methyl group or a hydroxymethyl group, R3 is one of a hydroxy group, a methoxy group, an ethoxy group, an isopropoxy group, a methoxyethoxy group, a methoxypropoxy group, or an ethoxypolopoxy group, and R4 is one of a hydroxy group, a methoxy group, an ethoxy group, an isopropoxy group, a methoxyethoxy group, a methoxypropoxy group, or an ethoxypolopoxy group. In particular, provided is a compound represented by the general formula [I] with R1 being a methyl group, R2 being a methyl group, R3 being a hydroxy group, and R4 being a methoxyethoxy group.

Abstract: The present invention discloses an aqueous pharmaceutical composition containing a protein in which serum albumin and growth hormone are linked. The aqueous pharmaceutical composition contains, as an active ingredient, a fusion protein of human serum albumin and human growth hormone; the concentration of the fusion protein is 10-100 mg/mL; the concentration of sucrose is 10-150 mg/mL; the concentration of a nonionic surfactant is 0.15-10 mg/mL; the concentration of a preservative is 0.5-12 mg/mL; the concentration of a buffer is 1-30 mM; and the pH is 5.0-8.0.

Abstract: Disclosed is a method for production of a fusion protein in which an antibody and a lysosomal enzyme are fused. The method comprises; (a) a step of culturing mammalian cells producing the fusion protein in a serum-free medium to let the mammalian cells secrete the fusion protein in the culture medium, (b) a step of collecting culture supernatant by removing the mammalian cells from the culture medium, and (c) a step of purifying the fusion protein from the culture supernatant by using a column chromatography employing as a solid phase a material to which a substance having affinity for the fusion protein has been bound, a column chromatography employing as a solid phase a material having affinity for the phosphate group, and a size exclusion column chromatography.

Abstract: A method for quantifying Hex4, lyso-GM1, Fuc-GlcNAc-Asn, or lyso-sulfatide included in cerebrospinal fluid, the method including adding an internal standard substance to a solution including the cerebrospinal fluid, submitting the solution including the cerebrospinal fluid, to which the internal standard substance has been added, to liquid chromatography to obtain an eluate, and subjecting the eluate to mass analysis.

Abstract: Disclosed are a means to convert compounds having physiological or pharmacological activity and unable to pass through the blood-brain barrier into a form that allows them to pass through the blood-brain barrier, and compounds converted thereby. The means is an anti-human transferrin receptor antibody and the converted compounds are molecular conjugates between physiologically active protein or pharmacologically active low-molecular-weight compounds and an anti-human transferrin receptor antibody.

Abstract: Disclosed are a means to convert compounds having physiological or pharmacological activity and unable to pass through the blood-brain barrier into a form that allows them to pass through the blood-brain barrier, and compounds converted thereby. The means is an anti-human transferrin receptor antibody and the converted compounds are molecular conjugates between physiologically active protein or pharmacologically active low-molecular-weight compounds and an anti-human transferrin receptor antibody.

Abstract: A filtration filter is configured from a first weld frame, a second weld frame, and a filter sandwiched and welded between the first weld frame and the second weld frame. The first weld frame and the second weld frame are configured by a flexible film having a film thickness of at least 120 ?m. The filter is configured by a substance having a higher melting point than the first weld frame and the second weld frame and having an opening area ratio of from 10% to 80%. The first weld frame is configured by a polymer that includes either a high density polyethylene having a melting point of from 120° C. to 140° C., a linear low density polyethylene having a melting point of from 105° C. to 125° C., or a mixture including at least one of the high density polyethylene or the linear low density polyethylene.