Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Method for animal ubiquitous expression of recombinant human lysozyme

A human lysozyme, systemic technology, applied in the field of obtaining new genes, can solve problems such as inability to achieve physical expression

Pending Publication Date: 2017-06-27
FOSHAN UNIVERSITY
View PDF3 Cites 3 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Even so, the human lysozyme obtained by the prior art is mainly expressed in the mammary gland, and cannot be expressed in multiple parts of the body

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

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Method for animal ubiquitous expression of recombinant human lysozyme
  • Method for animal ubiquitous expression of recombinant human lysozyme
  • Method for animal ubiquitous expression of recombinant human lysozyme

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 3

[0080] Example 3: Detection of biological activity of recombinant human lysozyme in serum

[0081] A. Agar plate method

[0082]Take 100uL Micrococcus lyticus respectively ( M. Lysodeikticus ) evenly spread on the 1.5% agar base broth culture plate, and put filter paper sheets with 10uL serum on the culture medium, the serum of ordinary mice is the negative control (NC), and the positive control is the standard product of human lysozyme. PC is 1ug human lysozyme standard. Set up 4 repetitions, culture at 28°C for 36 hours, observe the diameter of the inhibition zone, and visually judge the expression level and activity of recombinant human lysozyme ( image 3 .C).

[0083] The results showed that the serum samples of No. 1-7 F2 generation transgenic mice could all produce obvious inhibition zones, indicating that the recombinant human lysozyme had biological activity.

[0084] , Nephelometric method

[0085] Micrococcus lyticus was cultured in liquid medium for 24 hours,...

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

No PUM Login to View More

Abstract

The invention discloses a method for animal ubiquitous expression of recombinant human lysozyme. The method is characterized by comprising the following steps: I, performing human lysozyme BAC cloning, namely, selecting human lysozyme of the Genome Systems company as target hLZ BAC cloning, wherein the GenBank number of the human lysozyme is RP11-72P21; II, removing redundant gene CPSF6, namely, to avoid interference of the redundant gene CPSF6 to the hLZ gene, removing the redundant gene CPSF6 by using a recombinant method, thereby obtaining the human lysozyme pBAC-hLZ-Neo of which the redundant gene is removed. Compared with the prior art, the method has the advantages that the human lysozyme is expressed at multiple parts of bodies. The recombinant human lysozyme expressed in different tissue organs all have bioactivity, the number of bifidobacteria can be remarkably increased (P is less than 0.001) due to the recombinant human lysozyme expressed in intestinal tracts, and meanwhile the number of salmonella can be remarkably reduced (P is less than 0.001).

Description

technical field [0001] The present invention relates to a technique for obtaining new genes through recombination. Background technique [0002] Lysozyme, also known as mureinase or N-acetyl murein hydrolase, is an alkaline enzyme that can hydrolyze mucopolysaccharides in pathogenic bacteria. Mainly by destroying the β-1,4 glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in the cell wall, the insoluble mucopolysaccharides in the cell wall are decomposed into soluble glycopeptides, resulting in the escape of the contents of the cell wall Bacteria dissolve. Lysozyme can also directly combine with negatively charged viral proteins, and form double salts with DNA, RNA, and apoproteins to inactivate the virus. Therefore, the enzyme has antibacterial, anti-inflammatory, antiviral and other effects. [0003] At present, the lysozyme that is closely related to human life is mainly egg white lysozyme, which is widely derived from poultry egg white. It has a wid...

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 Applications(China)
IPC IPC(8): C12N15/85C12N9/36
CPCA01K2227/105A01K2267/01C12N9/2462C12N15/8509C12N2800/107C12Y302/01017
Inventor 刘燊鲁丹王晔张辉华林树茂黄得纯
Owner FOSHAN UNIVERSITY
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com