WO2023010682A1 - Anticorps capable de détecter une protéine d'agglutinine de nicotiana tabacum, procédé de préparation et son application - Google Patents
Anticorps capable de détecter une protéine d'agglutinine de nicotiana tabacum, procédé de préparation et son application Download PDFInfo
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- WO2023010682A1 WO2023010682A1 PCT/CN2021/123450 CN2021123450W WO2023010682A1 WO 2023010682 A1 WO2023010682 A1 WO 2023010682A1 CN 2021123450 W CN2021123450 W CN 2021123450W WO 2023010682 A1 WO2023010682 A1 WO 2023010682A1
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- WO
- WIPO (PCT)
- Prior art keywords
- emulsion
- immunization
- animal
- lectin protein
- antigen
- Prior art date
Links
- 238000002360 preparation method Methods 0.000 title claims abstract description 28
- 235000002637 Nicotiana tabacum Nutrition 0.000 title claims description 59
- 101710186708 Agglutinin Proteins 0.000 title abstract description 8
- 101710146024 Horcolin Proteins 0.000 title abstract description 8
- 101710189395 Lectin Proteins 0.000 title abstract description 8
- 101710179758 Mannose-specific lectin Proteins 0.000 title abstract description 8
- 101710150763 Mannose-specific lectin 1 Proteins 0.000 title abstract description 8
- 101710150745 Mannose-specific lectin 2 Proteins 0.000 title abstract description 8
- 244000061176 Nicotiana tabacum Species 0.000 title description 3
- 239000000839 emulsion Substances 0.000 claims abstract description 42
- 230000003053 immunization Effects 0.000 claims abstract description 42
- 238000002649 immunization Methods 0.000 claims abstract description 42
- 241001465754 Metazoa Species 0.000 claims abstract description 33
- 238000000034 method Methods 0.000 claims abstract description 15
- 238000011091 antibody purification Methods 0.000 claims abstract description 5
- 241000208125 Nicotiana Species 0.000 claims description 56
- 102000004856 Lectins Human genes 0.000 claims description 52
- 108090001090 Lectins Proteins 0.000 claims description 52
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 claims description 45
- 239000000872 buffer Substances 0.000 claims description 39
- 239000000427 antigen Substances 0.000 claims description 31
- 102000036639 antigens Human genes 0.000 claims description 31
- 108091007433 antigens Proteins 0.000 claims description 31
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 16
- 239000002671 adjuvant Substances 0.000 claims description 16
- 238000004587 chromatography analysis Methods 0.000 claims description 12
- 239000000203 mixture Substances 0.000 claims description 10
- 210000002966 serum Anatomy 0.000 claims description 10
- 239000006228 supernatant Substances 0.000 claims description 9
- 239000004471 Glycine Substances 0.000 claims description 8
- 150000001413 amino acids Chemical group 0.000 claims description 7
- 239000007853 buffer solution Substances 0.000 claims description 7
- 238000010828 elution Methods 0.000 claims description 6
- 102000004169 proteins and genes Human genes 0.000 claims description 6
- 108090000623 proteins and genes Proteins 0.000 claims description 6
- 238000010254 subcutaneous injection Methods 0.000 claims description 5
- 239000007929 subcutaneous injection Substances 0.000 claims description 5
- 239000012141 concentrate Substances 0.000 claims description 3
- 238000000703 high-speed centrifugation Methods 0.000 claims description 3
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 2
- 238000002347 injection Methods 0.000 claims description 2
- 239000007924 injection Substances 0.000 claims description 2
- 238000004108 freeze drying Methods 0.000 claims 1
- 239000002953 phosphate buffered saline Substances 0.000 claims 1
- 239000000910 agglutinin Substances 0.000 abstract description 4
- 238000002331 protein detection Methods 0.000 abstract description 2
- 239000000243 solution Substances 0.000 description 13
- 238000012546 transfer Methods 0.000 description 11
- 241000699670 Mus sp. Species 0.000 description 10
- 239000012528 membrane Substances 0.000 description 10
- 238000005406 washing Methods 0.000 description 9
- 239000007788 liquid Substances 0.000 description 8
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 8
- 239000002523 lectin Substances 0.000 description 7
- KWYHDKDOAIKMQN-UHFFFAOYSA-N N,N,N',N'-tetramethylethylenediamine Chemical compound CN(C)CCN(C)C KWYHDKDOAIKMQN-UHFFFAOYSA-N 0.000 description 4
- ROOXNKNUYICQNP-UHFFFAOYSA-N ammonium persulfate Chemical compound [NH4+].[NH4+].[O-]S(=O)(=O)OOS([O-])(=O)=O ROOXNKNUYICQNP-UHFFFAOYSA-N 0.000 description 4
- 230000000903 blocking effect Effects 0.000 description 4
- 239000008367 deionised water Substances 0.000 description 4
- 229910021641 deionized water Inorganic materials 0.000 description 4
- 238000001962 electrophoresis Methods 0.000 description 4
- 239000003292 glue Substances 0.000 description 4
- 239000004033 plastic Substances 0.000 description 4
- 229920003023 plastic Polymers 0.000 description 4
- 235000018102 proteins Nutrition 0.000 description 4
- 241000283707 Capra Species 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 241000607479 Yersinia pestis Species 0.000 description 3
- 238000009835 boiling Methods 0.000 description 3
- 239000005018 casein Substances 0.000 description 3
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 3
- 235000021240 caseins Nutrition 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- UQLDLKMNUJERMK-UHFFFAOYSA-L di(octadecanoyloxy)lead Chemical compound [Pb+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O UQLDLKMNUJERMK-UHFFFAOYSA-L 0.000 description 3
- 239000012160 loading buffer Substances 0.000 description 3
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 2
- 239000002033 PVDF binder Substances 0.000 description 2
- 229920002684 Sepharose Polymers 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 229910001870 ammonium persulfate Inorganic materials 0.000 description 2
- 239000011248 coating agent Substances 0.000 description 2
- 238000000576 coating method Methods 0.000 description 2
- 238000004042 decolorization Methods 0.000 description 2
- 239000003085 diluting agent Substances 0.000 description 2
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 238000011166 aliquoting Methods 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- UDSAIICHUKSCKT-UHFFFAOYSA-N bromophenol blue Chemical compound C1=C(Br)C(O)=C(Br)C=C1C1(C=2C=C(Br)C(O)=C(Br)C=2)C2=CC=CC=C2S(=O)(=O)O1 UDSAIICHUKSCKT-UHFFFAOYSA-N 0.000 description 1
- 238000004737 colorimetric analysis Methods 0.000 description 1
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 229910002804 graphite Inorganic materials 0.000 description 1
- 239000010439 graphite Substances 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 229930014626 natural product Natural products 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 230000010412 perfusion Effects 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 239000012089 stop solution Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000008399 tap water Substances 0.000 description 1
- 235000020679 tap water Nutrition 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/16—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from plants
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/06—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies from serum
- C07K16/065—Purification, fragmentation
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/415—Assays involving biological materials from specific organisms or of a specific nature from plants
- G01N2333/42—Lectins, e.g. concanavalin, phytohaemagglutinin
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change
Definitions
- the invention relates to the technical field of tobacco lectin protein detection, in particular to an antibody capable of detecting tobacco lectin protein and its preparation method and application.
- Tobacco lectin (Nictaba, Nicotiana tabacum agglutinin) was isolated from tobacco leaves for the first time in 2002, and it is an effective substance that can control various diseases and insect pests. Although there are very few related studies in China at present, a new research direction of using Nictaba as a carrier and using tobacco natural products for pest control is slowly being formed abroad. Tobacco lectins are distributed in various parts of the tobacco plant; the content of Nictaba is higher in the leaves, however, its presence is not detectable in all tobacco varieties.
- the present invention firstly provides a method for preparing an antibody capable of detecting tobacco lectin protein; the antibody prepared by the method has high specificity for detecting tobacco lectin protein, and can be used for detecting tobacco lectin protein, for The detection of tobacco lectins provides a new way.
- a method for preparing an antibody capable of detecting tobacco lectin protein comprising the following steps:
- Preparation steps of emulsion 1 mix antigen, Freund's complete adjuvant and PBS (specifically 0.01M PBS) to prepare antigen-containing emulsion 1;
- Preparation steps of emulsion 2 mix antigen, Freund's incomplete adjuvant and PBS (specifically 0.01M PBS) to prepare antigen-containing emulsion 2;
- the immunization step includes injecting the emulsion 1 into the animal to immunize the animal for the first time; after the first immunization, injecting the emulsion 2 into the animal to immunize the animal for the second time; After the immunization, inject the emulsion 2 into the animal to immunize the animal for the third time; and/or after the third immunization, inject the emulsion 2 into the animal to immunize the animal for the fourth time;
- Antibody purification step taking animal serum and purifying the antibody from the serum to obtain the antibody that can detect tobacco lectin protein;
- amino acid sequence of the antigen in emulsion 1 and emulsion 2 is shown in SEQ ID NO: 1.
- the dosage ratio of antigen, Freund's complete adjuvant and PBS is 300-500ug: 1mL: 1mL;
- the dosage ratio of antigen, Freund's incomplete adjuvant and PBS is 300-500ug:1mL:1mL.
- the dosage ratio of antigen, Freund's complete adjuvant and PBS is 400ug:1mL:1mL.
- the dosage ratio of antigen, Freund's incomplete adjuvant and PBS is 400ug:1mL:1mL.
- the amount of injected antigen is 40-60ug.
- the amount of injected antigen is 50ug/bird.
- the injection mentioned in the immunization step refers to subcutaneous injection.
- the animals in the immunization step are mice.
- the time for the first immunization is 2-3 weeks; the time for the second immunization is 2 weeks; the time for the third immunization is 1 week; the time for the fourth immunization is 1 week.
- Emulsion 1 and Emulsion 2 to immunize mice with the above steps four times, higher titers of antibodies that can detect tobacco lectin protein can be obtained.
- the antibody purification step specifically includes:
- the inventors have shown through a large number of studies that: high-purity antibodies that can detect tobacco lectin protein can be obtained by using the above chromatography column method.
- the PBS buffer containing citric acid described in step (3) refers to the PBS buffer containing 0.1M citric acid
- the PBS buffer solution containing citric acid and glycine refers to the PBS buffer solution containing 0.7M citric acid and 0.3M glycine.
- the composition of the PBS buffer plays a crucial role in the preparation of high-purity detectable tobacco lectin protein antibodies; when using PBS buffer containing 0.1M citric acid for washing When deactivated, high purity and high titer antibodies that can detect tobacco lectin protein can be obtained by enrichment. Further studies have shown that: when eluted with PBS buffer containing 0.7M citric acid and 0.3M glycine, antibodies that can detect tobacco lectin protein with higher purity and higher titer can be enriched.
- the present invention also provides an antibody capable of detecting tobacco lectin protein prepared by the above preparation method.
- the antibody capable of detecting tobacco lectin protein has the amino acid sequence described in SEQ ID NO: 2 or/and SEQ ID NO: 3.
- the present invention also provides an application of the above-mentioned antibody capable of detecting tobacco lectin protein in detecting tobacco lectin protein.
- the present invention prepares for the first time an antibody that can detect tobacco lectin protein; the antibody that can detect tobacco lectin protein has high specificity for tobacco lectin protein; therefore, the present invention can be used
- the antibody that can detect tobacco lectin protein is used to detect tobacco lectin protein; the antibody that can detect tobacco lectin protein according to the present invention is successfully prepared, which provides a new detection approach for the detection of tobacco lectin protein; in addition,
- the antibody capable of detecting tobacco lectin protein prepared by the method of the present invention also has high purity and titer; and the method is simple to operate and low in preparation cost.
- Example 1 Preparation of an antibody capable of detecting tobacco lectin protein
- the amount of antigen injected was 50ug/monkey; the time of the first immunization was 3 weeks; the time of the second immunization was 2 weeks; The time for the third immunization is 1 week; the time for the fourth immunization is 1 week;
- the antibody that can detect tobacco lectin protein can be obtained by lyophilizing the liquid.
- the antibody capable of detecting tobacco lectin protein has the amino acid sequence described in SEQ ID NO:2.
- Antigen coating Dilute the antigen with coating solution to the specified concentration (1ug/ml if not specified separately), add 100 ⁇ L/well into a polystyrene 96-well reaction plate, and place at 4°C overnight.
- Blocking add 200 ⁇ L/well blocking solution, and place at 37°C for 2 hours.
- Washing wash 5 times with washing liquid.
- Stop reaction, colorimetry add 50 ⁇ L/well stop solution. The color turns yellow; use a microplate reader to measure the absorbance of each well at 450 nm.
- the absorbance value in the measurement well of the test sample is more than 3 times the average value of the negative control well, which shows that the antibody prepared by the present invention that can detect the tobacco lectin protein is positive; and has a higher titer.
- Embodiment 3 Western Blot experiment
- separating gel solution with a concentration of 15%: add 2.3ml of deionized water, 5ml of 30% acrylamide, 2.5ml of Tris with a pH of 8.8, 100 ⁇ L of 10% ammonium persulfate, 100 ⁇ L of 10% SDS, and 6 ⁇ L of TEMED (add TEMED After that, the separating gel starts to polymerize immediately, so it should be mixed immediately and quickly);
- blocking solution is 1% casein or 2% OVA
- Example 1 reacts with the tobacco lectin protein and does not react with the empty vector, and the blank control group does not react with the tobacco lectin protein; this shows that the antibody prepared in Example 1 has no effect on tobacco agglutinin. Proteins are specific.
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Immunology (AREA)
- Organic Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Biophysics (AREA)
- Hematology (AREA)
- Urology & Nephrology (AREA)
- Biomedical Technology (AREA)
- Genetics & Genomics (AREA)
- Microbiology (AREA)
- Cell Biology (AREA)
- Biotechnology (AREA)
- Botany (AREA)
- Food Science & Technology (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Peptides Or Proteins (AREA)
Abstract
La présente invention se rapporte au domaine technique de la détection d'une protéine d'agglutinine de nicotiana tabacum, et concerne spécifiquement un anticorps capable de détecter une protéine d'agglutinine de nicotiana tabacum, son procédé de préparation et une application de celui-ci. Le procédé de préparation comprend les étapes suivantes : une étape de préparation pour une émulsion 1 ; une étape de préparation pour une émulsion 2 ; une étape d'immunisation, comprenant : l'injection de l'émulsion 1 dans un corps animal pour effectuer une première immunisation sur l'animal ; une fois que la première immunisation est terminée, l'injection de l'émulsion 2 dans le corps animal pour effectuer une seconde immunisation sur l'animal ; une fois que la seconde immunisation est terminée, l'injection de l'émulsion 2 dans le corps animal pour effectuer une troisième immunisation sur l'animal ; et/ou une fois que la troisième immunisation est terminée, l'injection de l'émulsion 2 dans le corps animal pour réaliser une quatrième immunisation sur l'animal ; et une étape de purification d'anticorps. L'anticorps préparé par le procédé présente une spécificité élevée pour la mesure d'une protéine d'agglutinine de nicotiana tabacum, et peut être utilisé pour détecter une protéine d'agglutinine de la nicotiana tabacum, ce qui permet d'obtenir une nouvelle manière de détecter l'agglutinine de la nicotiana tabacum.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202110898359.5A CN113603772B (zh) | 2021-08-05 | 2021-08-05 | 一种可检测烟草凝集素蛋白的抗体及其制备方法和应用 |
| CN202110898359.5 | 2021-08-05 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| WO2023010682A1 true WO2023010682A1 (fr) | 2023-02-09 |
Family
ID=78307222
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| PCT/CN2021/123450 WO2023010682A1 (fr) | 2021-08-05 | 2021-10-13 | Anticorps capable de détecter une protéine d'agglutinine de nicotiana tabacum, procédé de préparation et son application |
Country Status (2)
| Country | Link |
|---|---|
| CN (1) | CN113603772B (fr) |
| WO (1) | WO2023010682A1 (fr) |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101985475A (zh) * | 2009-07-28 | 2011-03-16 | 复旦大学附属华山医院 | 新型分泌肽inm02的多克隆抗体及其制备方法和应用 |
| CN104861059A (zh) * | 2015-04-29 | 2015-08-26 | 中国计量学院 | 一种褐飞虱vrg多肽及其多抗制备方法 |
| CN106432453A (zh) * | 2016-08-23 | 2017-02-22 | 广东省农业科学院作物研究所 | 一种烟草凝集素蛋白及其编码基因和应用 |
| CN109897090A (zh) * | 2018-12-24 | 2019-06-18 | 中国计量大学 | 一种褐飞虱Vg多肽及其多抗制备方法 |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20210386820A1 (en) * | 2018-09-06 | 2021-12-16 | Academia Sinica | Antiviral lectin and uses thereof |
| GB201903244D0 (en) * | 2019-03-14 | 2019-04-24 | Syndermix Ag | Methods for lectin production with improved yield |
| CN110938120B (zh) * | 2019-12-04 | 2021-12-03 | 中国农业科学院农业基因组研究所 | 改变二倍体马铃薯材料自交不亲和性的StSCI蛋白 |
-
2021
- 2021-08-05 CN CN202110898359.5A patent/CN113603772B/zh active Active
- 2021-10-13 WO PCT/CN2021/123450 patent/WO2023010682A1/fr unknown
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101985475A (zh) * | 2009-07-28 | 2011-03-16 | 复旦大学附属华山医院 | 新型分泌肽inm02的多克隆抗体及其制备方法和应用 |
| CN104861059A (zh) * | 2015-04-29 | 2015-08-26 | 中国计量学院 | 一种褐飞虱vrg多肽及其多抗制备方法 |
| CN106432453A (zh) * | 2016-08-23 | 2017-02-22 | 广东省农业科学院作物研究所 | 一种烟草凝集素蛋白及其编码基因和应用 |
| CN109897090A (zh) * | 2018-12-24 | 2019-06-18 | 中国计量大学 | 一种褐飞虱Vg多肽及其多抗制备方法 |
Non-Patent Citations (1)
| Title |
|---|
| LANNOO N., PEUMANS W., DAMME E.: "The presence of jasmonate-inducible lectin genes in some but not all Nicotiana species explains a marked intragenus difference in plant responses to hormone treatment", JOURNAL OF EXPERIMENTAL BOTANY, vol. 57, no. 12, GB , pages 3145 - 3155, XP093031812, ISSN: 0022-0957, DOI: 10.1093/jxb/erl076 * |
Also Published As
| Publication number | Publication date |
|---|---|
| CN113603772A (zh) | 2021-11-05 |
| CN113603772B (zh) | 2023-08-04 |
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