10 results about "Hexosamines" patented technology

Aspects of the disclosure relate to bicistronic AAV nucleic acid constructs comprising a transgene encoding hexosaminidase A (HEXA) and hexosaminidase (HEXB) proteins. In some embodiments, the disclosure provides methods for treating or preventing lysosomal storage disorders, such as Tay-Sachs disease and Sandhoff disease, using bicistronic nucleic acid constructs described by the disclosure.

The present disclosure provides a combination comprising an antibody that specifically binds to C5 and a C5 iRNA, which is a glycoconjugate containing a ligand with a terminal N-acetylgalactosamine (GalNAc) residue and / or N-acetylglucosamine (GlcNAc) residue. A method for reducing degradation of glycoconjugate RNA by the beta-hexosaminidase enzyme is also provided. The present disclosure also includes a method for treating or preventing a C5-related disease or disorder by administering one or more doses of an anti-C5 antibody or antigen-binding fragment thereof in combination with one or more doses of a C5 iRNA; preferably, the anti-C5 antibody or fragment and the C5 iRNA are in a combination. The present disclosure also includes a dosing regimen for treating a C5-related disease or disorder with a combination of an anti-C5 antibody and a C5 iRNA in either a treatment-naive subject or a subject switching from a previous C5 inhibitor therapy.

The present invention relates to nucleic acid constructs comprising a first polynucleotide encoding a signal peptide from a bacterial alpha-amylase a second polynucleotide encoding a polypeptide having hexosaminidase activity; expression vectors and host cells comprising said nucleic acid constructs; and methods for producing polypeptides having hexosaminidase activity.

The application provides application of biomarkers in preparation of products for diagnosing systemic lupus erythematosus, and belongs to the field of biological medicine. The biomarkers include C3_N85-HexNAc(2)Hex(1); C3 is complement C3, the amino acid sequence of which is shown as SED ID NO.3; N is an amino acid residue, and the number after N is a site; HexNAc is a hexosamine residue, Hex is a hexose residue, NeuAc is a sialic acid residue, and the number in the bracket represents the number of corresponding monosaccharide residues. The biomarkers also include at least one of F2_N121-HexNAc(2)Hex(12), VTN_N169-HexNAc(2)Hex(4) and APOB_N1523-HexNAc(3)Hex(4)NeuAc(1). The application proposes that the above protein N-glycopeptide is used as a biomarker for diagnosing SLE, has the advantages of high accuracy, high sensitivity and high specificity, and provides a new target for diagnosis and intervention improvement of SLE patients.

The present invention relates to a method for the synthesis of 6-azido-6-deoxy-2-N-acetyl-monosaccharide-nucleotide diphosphates, in particular 6-azido-6-deoxy-2-N-acetyl-D-galactosamine-nucleotide diphosphate or 6-azido-6-deoxy-2-N-acetyl-D-glucosamine-nucleotide diphosphate. The synthesis method according to the present invention is characterized by high efficiency and high yield. Another part of the present invention is a key intermediate of the method.

The present invention relates to compositions such as detergent or cleaning compositions comprising a polypeptide having hexosaminidase activity and a polypeptide having protease activity, as well as methods of using the compositions for e.g. laundry.

The present invention relates to a method of producing a polypeptide having β-hexosaminidase activity, comprising the steps of a) providing a yeast cell comprising a polynucleotide encoding a polypeptide having β-hexosaminidase activity and having an amino acid sequence being at least 95% identical to the amino acid sequence shown in SEQ ID NO: 1, b) cultivating said yeast cell under conditions which allow for the production of the polypeptide, and c) obtaining the polypeptide produced in step b). The present invention further concerns a polynucleotide encoding a polypeptide having β-hexosaminidase activity and having an amino acid sequence being at least 95% identical to the amino acid sequence shown in SEQ ID NO: 1, as well as polypeptide encoded by said polynucleotide. Moreover, the present invention concerns a yeast cell comprising the polynucleotide of the present invention.

To provide an improved method for producing a sugar nucleoside diphosphate in the field of a functionalized nucleoside sugar.SOLUTION: A method for the chemical conversion of GalNAc or GlcNAc to its respective 6-azido derivative via a cyclic sulfate, followed by conversion to the respective UDP derivative via an anomeric phosphorylation step and a UMP coupling step, wherein a 6-azido-6-deoxy monosaccharide compound having the structure (I) is prepared according to the following scheme: SELECTED DRAWING: None

This invention relates to a method for synthesizing 6-azido-6-deoxy-2-N-acetyl-monosaccharide-nucleoside diphosphate, particularly 6-azido-6-deoxy-2-N-acetyl-D-galactosamine-nucleoside diphosphate or 6-azido-6-deoxy-2-N-acetyl-D-glucosamine-nucleoside diphosphate. The synthetic method according to the invention is characterized by high efficiency and high yield. Another part of the invention concerns the key intermediates of this method.

This invention provides β-N-acetylglucosaminease mutants with improved thermal stability and catalytic performance, along with their screening methods and applications, relating to the field of enzyme engineering. This invention comprehensively utilizes X-ray crystal structure, AlphaFold2 and AlphaFold3 predicted structures, combined with ΔΔG... fold Computational analysis, sequence conservation analysis, B-factor flexible residue screening, and disulfide bond engineering were used to screen and combine beneficial mutations, resulting in the combinatorial mutant M9. Compared to the cbHEX synergistic system, the M9 synergistic system showed a 26.7-fold increase in monosaccharide yield and a 28% increase in crystalline chitin degradation rate. The strategy described in this invention can significantly improve the thermal stability and catalytic performance of the target enzyme and can provide a methodological reference for the rational modification of enzyme molecules.