91 results about "Acetylgalactosamine" patented technology

Methods and compositions for making glycoproteins, both in vitro and in vivo, are provided. One method involves incorporating an unnatural amino acid having a N-acetylgalactosamine moiety into a protein; optionally, the N-acetylgalactosamine-containing unnatural amino acid can be further modified with additional sugars.

A method for producing a chondroitin sugar chain comprises at least the following step: a step of allowing “a glucuronic acid donor”, “an N-acetyl galactosamine donor”, “a sugar receptor” and “a bacterial cell enzyme which synthesizes chondroitin” to coexist in a reaction system in the presence of a surfactant. Here, the surfactant is preferably selected from n-nonyl-β-D-thiomaltopyranoside, sucrose monocaproate and sucrose monolaurate. The chondroitin sugar chain has all the following properties 1) to 3): 1) a weight average molecular weight: 50,000 or more when it is measured by gel filtration chromatography, 2) it is completely degraded to disaccharides with chondroitinase ABC, 3) when the sugar chain is decomposed with chondroitinase ABC and the decomposed products are subjected to a disaccharide analysis, substantially all of them correspond to an unsaturated disaccharide unit of chondroitin.

The invention relates to the field of biological medicine, and in particular relates to liver targeted medicine. The medicine is chemical micromolecular medicine connecting galactosamine. The chemicalmicromolecular medicine is medicine for treating liver diseases or liver-related diseases. The chemical micromolecular medicine is prepared from but not limited to thyroxine T3, sorafenib, taxol, regorafenib, lamivudine, entecavir, telbivudine, statins, fibrates, niacin, bile acid sequestrants, other hepatitis virus DNA (RNA) polymerase inhibition compounds and the like. The galactosamine is tervalent acetylgalactosamine. The connection is the direct connection of the galactosamine and the chemical micromolecular medicine or the connection through linking fragments; the linking fragments comprise but not limited to carbon chains, disulfide bonds, pyrophosphate diester, cysteic acid, polypeptide and thioether or valine-citrulline. The medicine provided by the invention has the advantages that the liver targeted performance is improved; the medicine curative effect is enhanced; the toxic and side reactions on other non-targeted tissues are few.

A method for producing lacto-N-biose I and galacto-N-biose inexpensively and conveniently is provided. The method for producing lacto-N-biose I or galacto-N-biose, characterized in that the method comprises causing: (i) a combination of a carbohydrate raw material with an enzyme that catalyzes phosphorolysis of the carbohydrate raw material to give a-glucose-1-phosphate; and (ii) a combination of an enzyme that converts α-glucose-1-phosphate to UDP-glucose and an enzyme that converts UDP-galactose to galactose-1-phosphate with their cofactors, and/or a combination of an enzyme (UDP-Gly synthase) that converts α-glucose-1-phosphate and UDP-galactose to UDP-glucose and α-galactose-1-phosphate, respectively, with its cofactor(s) to act in the presence of N-acetylglucosamine or N-acetylgalactosamine, phosphoric acid, lacto-N-biose phosphorylase (EC 2.4.1.211), and UDP-glucose-4-epimerase (EC 5.1.3.2).

A human-derived novel chondroitin synthase, which is an enzyme for synthesizing a fundamental backbone of chondroitin and has both glucuronic acid transferring activity and N-acetylgalactosamine transferring activity.

The present invention examined the accumulation of chondroitin sulfate proteoglycans (CSPGs). The present invention relates to neurodegeneration-suppressing agents that are suitable for gene therapy or prevention of neural fibrotic degenerative diseases which induce neural cell death due to an accumulation of abnormal proteins, where the therapies are based on siRNAs against N-acetylgalactosamine-4-O-sulfotransferases (N-acetylgalactosamine-4-O-sulfotransferase-1, N-acetylgalactosamine-4-O-sulfotransferase-2, and N-acetylgalactosamine-4-sulfate 6-O-sulfotransferase (GalNAc4ST-1, GalNAc4ST-2, and GALNAC4S-6ST, respectively)), which are sulfotransferases for acetylgalactosamine, a CSPG side chain, and chondroitinase ABC, an enzyme that degrades chondroitin sulfate, another CSPG side chain.

Provided herein are oligomeric compounds with conjugate groups targeting apoplipoprotein C-III (ApoCIII). In certain embodiments, the ApoCIII targeting oligomeric compounds are conjugated to N-Acetylgalactosamine. Also disclosed herein are conjugated oligomeric compounds targeting ApoCIII for use in decreasing ApoCIII to treat, prevent, or ameliorate diseases, disorders or conditions related to ApoCIII. Certain diseases, disorders or conditions related to ApoCIII include inflammatory, cardiovascular and/or metabolic diseases, disorders or conditions. The conjugated oligomeric compounds disclosed herein can be used to treat such diseases, disorders or conditions in an individual in need thereof.

Provided herein are oligomeric compounds with conjugate groups targeting apoplipoprotein (a) [apo(a)]. In certain embodiments, the apo(a) targeting oligomeric compounds are conjugated to N-Acetylgalactosamine. Also disclosed herein are conjugated oligomeric compounds targeting apo(a) for use in decreasing apo(a) to treat, prevent, or ameliorate diseases, disorders or conditions related to apo(a) and/or Lp(a). Certain diseases, disorders or conditions related to apo(a) and/or Lp(a) include inflammatory, cardiovascular and/or metabolic diseases, disorders or conditions. The conjugated oligomeric compounds disclosed herein can be used to treat such diseases, disorders or conditions in an individual in need thereof.

The present invention provides a method for detecting a glycan structure of a prostate specific antigen (PSA) rapidly and with high sensitivity and determining prostate carcinoma based on the difference in the structure, in particular, a method for determining between prostate carcinoma and benign prostatic hyperplasia accurately. A method for determining prostate carcinoma, wherein the method includes a step of analyzing a PSA glycan structure in a sample derived from a test subject, and prostate carcinoma is determined in the case that amount of a glycan having LacdiNAc (N-acetylgalactosamine-N-acetylglucosamine) (LacdiNAc(+)) is more than 30% of amount of a glycan not having LacdiNAc but having LacNAc (galacotose-N-acetylglucosamine) (LacdiNAc(−)). Especially, a method for determining prostate carcinoma, wherein prostate carcinoma is determined in the case that amount of a glycan having LacdiNAc (N-acetylgalactosamine-N-acetylglucosamine) (LacdiNAc(+)) is more than 30% of amount of a glycan not having LacdiNAc but having LacNAc (galacotose-N-acetylglucosamine) (LacdiNAc(−)), and benign prostatic hyperplasia is determined in the case of 30% or less.

An enzyme which transfers N-acetylgalactosamine to N-acetylglucosamine via a β1-4 linkage was isolated and the structure of its gene was explained. This led to the production of said enzyme or the like by genetic engineering techniques, the production of oligosaccharides using said enzyme, and the diagnosis of diseases on the basis of said gene or the like. The present invention uses a protein having the amino acid sequence shown in SEQ ID NO: 1, 3, 26 or 27 in the Sequence Listing or a variant of said amino acid sequence wherein one or more acids are substituted or deleted, or one or more acids are inserted or added and having the activity of transferring N-acetylgalactosamine (GalNAc) to N-acetylglucosamine serving as a substrate via a β1-4 linkage and nucleic acids encoding said protein.

Provided are a method for producing a fraction containing more than 50% of CH represented by the general formula (1), which comprises at least the step of allowing a glucuronic acid donor, an N-acetylgalactosamine donor, a saccharide receptor, a chondroitin polymerase derived from the Escherichia coli K4 strain, and Mn²⁺ at a final concentration of 0.02 to 100 mM to coexist, and performing a reaction thereof under conditions of 20 to 40° C. and pH 6 to 8 for 0.5 minutes to 4 hours, and a method for producing a fraction containing more than 50% of CH represented by the general formula (2), which comprises at least the step of performing the reaction under same conditions for 10 hours or longer, which enable industrial scale production of a CH fraction of a controlled even number saccharide and odd number saccharide content ratio by a simple procedure at a low cost.

(GlcA-GalNAc)_n   (1)

GalNAc-(GlcA-GalNAc)_n   (2)

• (In the formula, GlcA represents a glucuronic acid residue, GalNAc represents a N-acetylgalactosamine residue, - represents a glycosidic bond, and n represents an arbitrary integer.)

The invention relates to a biological enzyme composite blocking remover and a preparation method thereof, which belong to the technical field of oil field yield increase renovation. The blocking remover comprises the following components by mass: 0.1-0.5% of biological enzyme, 3-5% of a biological surfactant, 5-10% of a biological enzyme stabilizer, and the balance of water; the biological enzyme comprises at least one of xylanase, lipase, cellulase, mannase, protein complex enzyme, amylase and xanthan gum lyase; the biological surfactant is prepared from at least one of the following components: the biological surfactant is mainly prepared from rhamnolipid, sophorolipid and N-acetylgalactosamine; and the biological enzyme stabilizer comprises at least one of the following components: disodium ethylene diamine tetraacetate, citric acid and triethanolamine. The biological enzyme composite blocking remover provided by the invention can solve the problems of permeability reduction and the like caused by low-permeability and medium-low-permeability reservoir reconstruction residual gum and organic matter (wax, asphaltene and the like) blocking in the later development period.

The invention discloses an α-N-acetylgalactosaminidase and its encoding gene and application. The α-N-acetylgalactosaminidase is a protein of the following (a) or (b): (a) a protein consisting of the amino acid sequence shown in SEQ ID NO: 3 in the sequence listing; A protein derived from (a) having α-N-acetylgalactosaminidase activity through the substitution and/or deletion and/or addition of one or several amino acid residues in the amino acid sequence. The α-N-acetylgalactosaminidase can change the blood type of human red blood cells from A to O, and from AB to B. αNAGA can be used to prepare kits for blood group conversion; αNAGA can also be used to prepare universal red blood cells.

The invention belongs to the technical field of biochemical analysis and detection, in particular to a detection method and a detection kit for acid hydrolase activity in lysosomes. The present invention firstly designs a detection system comprising 5 kinds of mucopolysaccharide acid hydrolase in lysosomes, these five kinds of enzymes are respectively: α-L-iduronidase, iduronate sulfatase, β-N-acetyl half Lactosamine‑6‑sulfatase, β‑galactosidase and arylsulfatase B enzymes. The present invention utilizes the characteristic of fluorescence of 4-methylumbelliferone, uses the new substrate produced by combining the 4-methylumbelliferone group obtained by chemical synthesis with the enzyme substrate, and adopts the acid buffer solution containing the new substrate and mucopolysaccharide The hydrolase reacts, and the free 4-methylumbelliferone fluorescent substance is released after the hydrolase hydrolyzes the substrate. The higher the activity of the hydrolase in the sample, the more the amount of 4-methylumbelliferone released by hydrolyzing the substrate, and the higher the fluorescence intensity generated by the fluorescence detection, so as to realize the quantitative detection of the hydrolase activity. The invention has high detection sensitivity, good selectivity, strong anti-interference ability, good reproducibility and easy operation.

The invention discloses a meat duck feed additive and a use thereof. The meat duck feed additive comprises, by weight, 5-10% of fucose, 5-10% of galactose, 10-15% of N-acetylgalactosamine, 5-15% of glucosamine, 5-10% of N-acetylglucosamine, 5-15% of glucuronic acid, 10-20% of mannose, 5-10% of sialic acid and 10-20% of xylose. A use ratio of the meat duck feed additive in meat duck daily basic feed is 0.001-5%. The meat duck feed additive is rich in biologically-active substances, can improve appetite and immunity, can prevent diseases, can promote meat duck growth and improve meat quality, has no toxic or side effect, does not produce residue and is green and safe.

The invention discloses a complex carbohydrate preparation for forage, a forage additive containing the complex carbohydrate preparation, and a use of the forage additive. The complex carbohydrate preparation comprises, by weight, 10-15 parts of fucose, 5-10 parts of galactose, 5-10 parts of N-acetylgalactosamine, 10-30 parts of glucosamine, 5-15 parts of N-acetylgalactosamine, 5-10 parts of glucuronic acid, 10-20 parts of mannose, 5-10 parts of sialic acid and 10-20 parts of xylose. The forage additive comprises, by weight, 65-140 parts of the complex carbohydrate preparation. The forage additive is added into basic daily forage according to a use ratio of 0.001-2% so that the forage for pregnant sows is obtained. The complex carbohydrate preparation improves sow constipation, improves pigling birth weight and sow lactation amount, provides a novel pregnant sow and lactating sow forage formula for actual production, improves production efficiency and culture benefits, has high safety, has no side effect, can adjust and balance various nutrients, prolongs a lactation period and is conducive to timely oestrus hybridization after sow weaning.