Unlock instant, AI-driven research and patent intelligence for your innovation.

Method for preparing glycopeptide isomer from ribonuclease b and glycopeptide isomer

A ribonuclease and isomer technology, applied in the preparation method of peptides, chemical instruments and methods, peptides, etc., can solve the problems of inability to separate and prepare glycopeptide isomers

Active Publication Date: 2020-07-07
DALIAN INST OF CHEM PHYSICS CHINESE ACAD OF SCI
View PDF2 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0003] For the separation of glycopeptides, currently developed methods include reversed-phase chromatography, affinity chromatography, hydrophilic chromatography, and two-dimensional chromatography such as strong cation exchange / reversed-phase chromatography, reversed-phase chromatography / graphitized carbon method, but At present, these methods are only used in conjunction with mass spectrometry to identify glycopeptides or glycopeptide isomers through the extraction of specific molecular weights by mass spectrometry, and cannot separate and prepare glycopeptide isomers

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0025] Weigh 1 mg of ribonuclease B protein (Sigma-Aldrich, product number R7884), add 167 μL of 4M urea in 30 mM ammonium bicarbonate buffer solution, incubate at 20°C for 1 hour, the pH of the buffer solution is 7. Add 15 μL of 30 mM dithiothreitol aqueous solution to the denatured ribonuclease B protein, and incubate at 35°C for 1 hour to reduce the disulfide bond of the denatured protein, then add 10 μL of 30 mM iodoacetic acid aqueous solution, under dark conditions Incubate at 30°C for 10 minutes to alkylate the reduced disulfide bonds.

[0026] Add denatured ribonuclease B to 960 μL ammonium bicarbonate buffer solution with a concentration of 0.1M; add 0.1 mg of Trypsin, the pH value of the enzymolysis buffer solution is 7, the enzymolysis reaction temperature is 35°C, and the enzymolysis time is 10 Hours, after enzymolysis, the enzymolysis solution was boiled in boiling water for 5 minutes to inactivate the enzyme. The enzymolysis solution was centrifuged and concentr...

Embodiment 2

[0028] Weigh 10 mg of ribonuclease B protein (Sigma-Aldrich, product number R7884), add 100 μL of 8M urea in 50 mM ammonium bicarbonate buffer solution, incubate at 30° C. for 5 hours, and the pH of the buffer solution is 9. Add 15 μL of 30 mM dithiothreitol aqueous solution to the denatured ribonuclease B, incubate at 40°C for 5 hours to reduce the disulfide bond of the denatured ribonuclease B, then add 6 μL of 50 mM iodoacetic acid aqueous solution, and keep away from light Incubate at 20°C for 60 minutes under conditions to alkylate the reduced disulfide bonds.

[0029] Add denatured ribonuclease B to 1210 μL of ammonium bicarbonate buffer solution at a concentration of 0.5M, add 0.2 mg of Trypsin, the pH of the enzymolysis buffer solution is 9, the enzymolysis reaction temperature is 40°C, and the enzymolysis time is After 24 hours of enzymolysis, the enzymolysis solution was boiled in boiling water for 10 minutes to inactivate the enzyme. The enzymatic hydrolysis soluti...

Embodiment 3

[0032] Weigh 30 mg of ribonuclease B protein (Sigma-Aldrich, product number R7884), add 100 μL of 10 M urea in 50 mM ammonium bicarbonate buffer solution, incubate at 25°C for 2 hours, the pH of the buffer solution is 7. Add 10 μL of 100 mM dithiothreitol aqueous solution to the denatured ribonuclease B, incubate at 37°C for 5 hours, reduce the disulfide bond of the denatured ribonuclease B, then add 25 μL of 100 mM iodoacetic acid aqueous solution, and keep away from light Incubate at 30°C for 20 minutes under conditions to alkylate the reduced disulfide bonds.

[0033] Add denatured ribonuclease B to 1500 μL of ammonium bicarbonate buffer solution with a concentration of 5M, add 1 mg of Trypsin, the pH of the enzymolysis buffer solution is 8, the enzymolysis reaction temperature is 37°C, and the enzymolysis time is 24 hours , after enzymolysis, the enzymolysis solution was boiled in boiling water for 5 minutes to inactivate the enzyme. The enzymatic hydrolysis solution was ...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

PropertyMeasurementUnit
particle diameteraaaaaaaaaa
particle diameteraaaaaaaaaa
particle diameteraaaaaaaaaa
Login to View More

Abstract

The present invention provides a method for separating and preparing glycopeptide isomers from ribonuclease B and the glycopeptide isomers, the main components of which are glycopeptide isomers whose peptide sequence is NLTK. After the ribonuclease B was digested by trypsin, it was centrifuged and concentrated, and the concentrated solution was removed from the salt, polypeptide and residual protein in the enzymatic hydrolysis solution by one-dimensional chromatographic column, and the target fraction was collected. The collected fractions were centrifuged and concentrated, and the concentrate was passed through a two-dimensional chromatographic column and combined with mass spectrometry. Under the guidance of mass spectrometry monitoring, separation and preparation were carried out to obtain two high-purity ribonuclease B glycopeptide isoforms with a molecular weight of 1852.75. Construct.

Description

technical field [0001] The present invention relates to a separation and preparation method for separating and preparing glycopeptide isomers from proteins, specifically, enzymatic separation and separation from ribonuclease B to obtain glycopeptide isomers whose peptide segment is NLTK, containing two N-acetyl Glucosamine and 5 mannose with a molecular weight of 1852.75. Background technique [0002] Protein glycosylation is an important post-translational modification of proteins. In eukaryotes, especially mammals, more than half of proteins are glycosylated (Apweiler R, Hermjakob H, Sharon N, On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim Biophys Acta-Gen Subj, 1999, 1473, 4-8). As a major post-translational modification of proteins, glycosylation has an important impact on the structure and function of proteins. The sugar chains of glycoproteins play an important role in the recognition, adhesion, communication an...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Patents(China)
IPC IPC(8): C12P21/06C07K1/16C07K9/00
Inventor 梁鑫淼付冬梅于龙卢俊肖远胜曹翠岩
Owner DALIAN INST OF CHEM PHYSICS CHINESE ACAD OF SCI