146 results about "Glycosylated protein" patented technology

The present invention relates to a prokaryotic host cell comprising eukaryotic glycosyltransferase activity, where the eukaryotic glycosyltransferase activity is eukaryotic dolichyl-linked UDP-GlcNAc transferase activity and eukaryotic mannosyl-transferase activity. Also disclosed is a method of producing a glycosylated protein by providing a prokaryotic host cell comprising the eukaryotic glycosyltransferase activity and culturing the prokaryotic host cell under conditions effective to produce a glycosylated protein. Another aspect of the present invention pertains to a method for screening bacteria or bacteriophages by expressing one or more glycans on the surface of a bacteria, attaching a label on the one or more glycans on the surface of the bacteria or on the surface of a bacteriophage derived from the bacteria, and analyzing the label in a high-throughput format. A glycosylated antibody comprising an Fv portion which recognizes and binds to a native antigen and an Fc portion which is glycosylated at a conserved asparagine residue is also disclosed.

This invention relates, e.g., to transgenic insects, or progeny thereof, whose cells contain at least one genomically integrated, expressible, nucleic acid encoding two or more of a set of Nglycosylation enzymes that can glycosylate a heterologous protein with a mammalianized (e.g., humanized) glycosylation pattern. The glycosylation genes are preferably expressed in the insect cells in catalytic amounts. Also described are methods to use such a transgenic insect to produce heterologous, mammalianized polypeptides of interest.

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.

The invention belongs to the technical field of chitosan oligosaccharide modification of proteins, and particularly, relates to a glycosylation method for improving the emulsification stability of aquatic collagen. The aquatic collagen is subjected to glycosylation modification by adopting chitosan oligosaccharide to obtain modified glycosylated collagen; in particular, the method comprises three steps of preparation of fish skin gelatin, glycosylated protein preparation, and purification and collection; transglutaminase (TG enzyme) is used for realizing chitosan oligosaccharide modification of the collagen, functional properties (including water absorption, gelation property, thermal stability and the like) of the chitosan can be improved, the collagen is allowed to have certain physiological activities (including activities of enhancing immunity, lowering blood pressure, lowering blood sugar, reducing cholesterol and the like), moreover, the problems generated in glycosylation modification of the protein through a Maillard reaction are solved, a protein ingredient having special functional properties is developed for food industries, and a new theoretical basis and a new technical method are provided.

The present invention provides an electrochemical detection method for content of glycosylated hemoglobin in the blood, and is characterized in that: whole blood specimen is diluted by combined liquid ranging from 30 times to 70 times and passes through a glycosylated protein recognizer, electric activated small molecules are filled into the effluent liquid from the glycosylated protein recognizer, and electrochemical response of the liquid is detected by chemically modified electrodes after the filling, thereby obtaining the concentration of the blood glucose. The glycosylated protein recognizer is eluted by elute solvent, and the electrochemical response of the elute solvent is detected and the concentration of the glycosylated hemoglobin is obtained, thereby obtaining the content of the glycosylated hemoglobin of the sample after calculation. As the electrochemical detection is simple in operation, lower in cost and rapid in the analysis, the present invention is expected to realize the rapid determination of the clinical glycosylated hemoglobin and the rapid determination of the glycosylated hemoglobin after separation and elution.

The invention discloses a novel protein glycosylation grafting method. The method comprises the following steps of: (1) adding buffer solution into a crowding reagent and stirring the mixture to obtain solution; and (2) adding protein and glucan into the solution obtained by the step (1), stirring the mixture for 2 hours, adding NaN3 into the mixture, placing the mixture for 24 hours at the temperature of 5 DEG C, stirring the mixture for 12 to 48 hours at the temperature of between 50 and 70 DEG C again and quickly cooling the mixture to the temperature of less than 25 DEG C to obtain a glycosylation protein product. The method has the advantages of greatly improving functional characters such as water solubility, emulsibility, antioxidation and the like of a graft, along with convenientoperation and high reaction efficiency; and the product has industrial and large-scale application prospect.

The present invention relates to an identification method for an O-glycosylation peptide fragment and a complete saccharide chain thereof. The technical process specifically comprises that a glycosylation protein sample is subjected to PNGase F digestion to remove N-glycosylation modification interference, enrichment is performed through hydrophilic interaction chromatography, and finally analysis is performed through time of flight mass spectrometer. According to the present invention, the method process has advantages of simple and rapid operation, high identification sensitivity, and the like; and the O-glycosylation peptide fragment and the complete saccharide chain thereof of the complex biological sample can be identified so as to achieve the research on the micro-uniformity of the O-glycosylation modification structure.

The present invention relates to methods and compositions for the identification of cancer markers. In particular, the present invention provides methods and compositions for the identification of glycosylated proteins and protein glycosylation patterns. The present invention further provides cancer markers identified using the described methods.

To analyze glycans and peptide sequences without liberating glycans from glycosylated peptides, a glycan structure is analyzed through negative-ion CID, in which sialic acid and fucose are resistant to elimination, and a peptide sequence is analyzed through positive-ion ECD.

The invention discloses application of lectin group recognized carbohydrate chains in distinguishing mucinous cystic neoplasm from serous cystic neoplasm. The lectin group recognized carbohydrate chains disclosed by the invention are glycosylated protein carbohydrate chains recognized by lectin groups consisting of WGA (trticum vulgaris agglutinin), BPL (bauhinia purpurea lectin), STL (solanum tuberosum (potato) lectin), DBA (dolchos biflorus agglutinin), PTL-I (psophocarpus tetragonolobus lectin I) and MAL-I (maackia amurensis lectin I). The carbohydrate chains are different in capsula pancreatic fluid of patients suffering from mucinous cystic neoplasm and serous cystic neoplasm, the contents of the carbohydrate chains recognized by STL, WGA, BPL and DBA in the capsula pancreatic fluid of patients suffering from MCN (mucinous cystic neoplasm) are remarkably higher than those in the capsula pancreatic fluid of patients suffering from SCN (serous cystic neoplasm), the contents of the carbohydrate chains recognized by PTL-I and MAL-I in the capsula pancreatic fluid of the patients suffering from MCN are remarkably lower than those in the capsula pancreatic fluid of the patients suffering from SCN, the sensitivity of the combination of WGA and BPL in distinguishing the patients suffering from SCN from the patients suffering from MCN is 0.714, and the specificity is 1. The results show that the lectin group can be used for distinguishing the patients from SCN from the patients suffering from MCN.

Production of non-glycosylated protein from yeast is carried out by constructing expression carrier containing N-glycoamidase and purposive protein gene from molecular biological technology, transferred into yeasts from electric transformation, expressing N- glycoamidase on yeast cell surface, excretory expressing purposive protein into culture medium, removing chain of glucoprotein excretory expressed from N- glycoamidase surface expressed and obtaining non-glycosylated protein. It has better expression protein activity and correct tertiary structure and no immunogenicity to human body.