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Apolipoprotein II/I and preparation method, biological function and application thereof

A technology of apolipoprotein and expression product, applied in the field of biomedicine, application field in the field of biomedicine

Active Publication Date: 2017-05-10
SHENYANG PHARMA UNIVERSITY
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0008] So far, there has been no related research on the structure, preparation, biological function and application of apolipoprotein II / I of Lepidoptera (Large) Mothidae insects

Method used

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  • Apolipoprotein II/I and preparation method, biological function and application thereof
  • Apolipoprotein II/I and preparation method, biological function and application thereof
  • Apolipoprotein II/I and preparation method, biological function and application thereof

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0087] Isolation and Purification of Natural apoLp-II / I

[0088] 1. Method 1

[0089] Collect the hemolymph, centrifuge at 12000×g and get the supernatant. Carry out 40% ammonium sulfate precipitation; centrifuge to take the precipitate and redissolve it with 50mM citric acid buffer solution pH5.2, 100mM NaCl, 5% glycerol; after centrifugation, take the supernatant, pass through Sephacryl S-200 column, and collect the effluent group containing the target protein After the fraction was dialyzed with 50mM PB pH8.0, it was eluted with a gradient of 0-1M NaCl on a HiTrapTM SP column, and the effluent fraction containing the target protein was collected.

[0090] Test results such as figure 1 -A Swimming lane 7, wherein arrow 1 points to apolipoprotein I, arrow 2 points to apolipoprotein II, and the purity of natural apoLp-II / I reaches electrophoretic purity.

[0091] 2. Method 2

[0092] Tussah hemolymph was precipitated with 70% ammonium sulfate, and then centrifuged at 8000×g ...

Embodiment 2

[0098] Analysis of apoLp-II / I structure and its gene sequence analysis

[0099] According to the techniques, methods and means of conventional protein chemistry and molecular biology, the structure analysis of apoLp-II / I was carried out. The specific methods and means are implemented according to the contents listed in the second content of the invention.

[0100] Obtain the complete nucleotide sequence of apoLp-II / I and its amino acid sequence (as shown in SEQ ID: 1 and ID: 2).

Embodiment 3

[0102] Obtaining Active Fragment of Recombinant apoLp-II / I Using Prokaryotic Expression System

[0103] This example lists and describes the construction strategy and basic method for expressing the apoLp-II / I active fragment gene of the present invention in a prokaryotic expression system.

[0104] The expression vector, expression host cell and expression strategy of the prokaryotic expression system are the conventional and general expression vector, expression host cell and expression strategy of genetic engineering expression.

[0105] This implementation is to enable those skilled in the art to understand the present invention more comprehensively, but not to limit the scope of the special claims of the present invention in any way.

[0106] For the separation and purification method of the expression product, the method, principle, strategy, etc. of Example 1 were adopted.

[0107] 1. Expression vector construction of apoLp-II / I active fragment

[0108] According to t...

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PUM

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Abstract

The invention relates to the technical field of biological medicines, and in particular to a structure of an apolipoprotein II / I and a preparation method, a new biological function and application thereof in the field of biological medicines. Specifically, the invention relates to the apolipoprotein II / I, the structure of an active fragment thereof, a preparation and production method and a function thereof, as well as application thereof in biological medicine fields, such as the test and diagnosis of microbes and associated molecular patterns, the promotion of the production of insect haemolymph melanin and the synthesis of antimicrobial peptides by inducing insects, the preparation of antibodies of the apolipoprotein II / I and the active fragment and application thereof in the field of biological medicines. The amino acid sequence of the apolipoprotein II / I disclosed by the invention is shown as SEQ ID: 2; and an gene sequence for coding the amino acid sequence of the apolipoprotein II / I is shown as SEQ ID: 1. The invention further provides a natural apolipoprotein II / I and a recombinant apolipoprotein II / I active fragment, shown as SEQ IDs: 3-6.

Description

[0001] Technical field: [0002] The invention relates to the technical field of biomedicine, and relates to the structure of the apolipoprotein II / I, its obtaining method, its new biological function and its application in the field of biomedicine. Specifically, the present invention relates to the structure of apolipoprotein II / I and its active fragments and its preparation and production methods and functions, as well as its detection and diagnosis in microorganisms and related molecular patterns, promotion of insect hemolymph melanin production, and induction of insect synthesis of antibacterial Peptides and other biomedical applications, preparation of apolipoprotein II / I and active fragment antibodies and their applications in the biomedical field. [0003] Background technique: [0004] Apolipoprotein is the protein part of plasma lipoprotein, and its basic function is to transport lipid substances and stabilize lipoprotein structure. Apolipoproteins are called apolipop...

Claims

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Application Information

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IPC IPC(8): C07K14/775C07K1/18C07K1/22C07K1/20C07K1/16C07K1/30C07K1/34C07K1/36C12N15/12C07K16/18G01N33/92
CPCC07K14/775C07K16/18G01N33/92G01N2333/775
Inventor 张嵘张景海吴春福
Owner SHENYANG PHARMA UNIVERSITY
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