CN104650200A - Plant protein with tumor antigenicity - Google Patents
Plant protein with tumor antigenicity Download PDFInfo
- Publication number
- CN104650200A CN104650200A CN201510038320.0A CN201510038320A CN104650200A CN 104650200 A CN104650200 A CN 104650200A CN 201510038320 A CN201510038320 A CN 201510038320A CN 104650200 A CN104650200 A CN 104650200A
- Authority
- CN
- China
- Prior art keywords
- protein
- vegetable
- centrifugal
- tumor
- precipitation
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
- 206010028980 Neoplasm Diseases 0.000 title claims abstract description 40
- 108010064851 Plant Proteins Proteins 0.000 title abstract 4
- 235000021118 plant-derived protein Nutrition 0.000 title abstract 4
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 18
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 18
- 238000000034 method Methods 0.000 claims abstract description 9
- 108010082495 Dietary Plant Proteins Proteins 0.000 claims description 27
- 239000000872 buffer Substances 0.000 claims description 15
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 claims description 12
- 235000019750 Crude protein Nutrition 0.000 claims description 10
- 238000001556 precipitation Methods 0.000 claims description 10
- 239000006228 supernatant Substances 0.000 claims description 10
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 claims description 9
- 239000002953 phosphate buffered saline Substances 0.000 claims description 9
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 claims description 7
- 229910052921 ammonium sulfate Inorganic materials 0.000 claims description 7
- 238000012870 ammonium sulfate precipitation Methods 0.000 claims description 7
- 235000011130 ammonium sulphate Nutrition 0.000 claims description 7
- 238000013467 fragmentation Methods 0.000 claims description 7
- 238000006062 fragmentation reaction Methods 0.000 claims description 7
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 claims description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 6
- 229910000147 aluminium phosphate Inorganic materials 0.000 claims description 6
- 238000010612 desalination reaction Methods 0.000 claims description 6
- 238000001514 detection method Methods 0.000 claims description 5
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 claims description 4
- 238000001962 electrophoresis Methods 0.000 claims description 4
- 239000007788 liquid Substances 0.000 claims description 4
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 claims description 4
- 239000000243 solution Substances 0.000 claims description 4
- 239000003814 drug Substances 0.000 claims description 3
- 238000000227 grinding Methods 0.000 claims description 3
- 229910052757 nitrogen Inorganic materials 0.000 claims description 3
- 238000012360 testing method Methods 0.000 claims description 3
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 claims description 2
- YVNQAIFQFWTPLQ-UHFFFAOYSA-O [4-[[4-(4-ethoxyanilino)phenyl]-[4-[ethyl-[(3-sulfophenyl)methyl]amino]-2-methylphenyl]methylidene]-3-methylcyclohexa-2,5-dien-1-ylidene]-ethyl-[(3-sulfophenyl)methyl]azanium Chemical compound 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)C=2C(=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S(O)(=O)=O)C)C=C1 YVNQAIFQFWTPLQ-UHFFFAOYSA-O 0.000 claims description 2
- 239000002253 acid Substances 0.000 claims description 2
- 150000001413 amino acids Chemical class 0.000 claims description 2
- 150000003863 ammonium salts Chemical class 0.000 claims description 2
- 238000011033 desalting Methods 0.000 claims description 2
- 239000012153 distilled water Substances 0.000 claims description 2
- 229940079593 drug Drugs 0.000 claims description 2
- 238000005374 membrane filtration Methods 0.000 claims description 2
- 238000011275 oncology therapy Methods 0.000 claims description 2
- 238000004073 vulcanization Methods 0.000 claims description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 2
- 210000004027 cell Anatomy 0.000 abstract description 27
- 206010006187 Breast cancer Diseases 0.000 abstract description 3
- 208000026310 Breast neoplasm Diseases 0.000 abstract description 3
- 206010009944 Colon cancer Diseases 0.000 abstract description 3
- 206010038389 Renal cancer Diseases 0.000 abstract description 2
- 208000006265 Renal cell carcinoma Diseases 0.000 abstract description 2
- 208000029742 colonic neoplasm Diseases 0.000 abstract description 2
- 206010017758 gastric cancer Diseases 0.000 abstract description 2
- 206010073071 hepatocellular carcinoma Diseases 0.000 abstract description 2
- 201000010174 renal carcinoma Diseases 0.000 abstract description 2
- 206010041823 squamous cell carcinoma Diseases 0.000 abstract description 2
- 210000004881 tumor cell Anatomy 0.000 abstract description 2
- 201000009030 Carcinoma Diseases 0.000 abstract 1
- 208000019065 cervical carcinoma Diseases 0.000 abstract 1
- 239000000284 extract Substances 0.000 abstract 1
- 208000010749 gastric carcinoma Diseases 0.000 abstract 1
- 235000018102 proteins Nutrition 0.000 abstract 1
- 230000002685 pulmonary effect Effects 0.000 abstract 1
- 201000000498 stomach carcinoma Diseases 0.000 abstract 1
- 238000012795 verification Methods 0.000 abstract 1
- 210000001519 tissue Anatomy 0.000 description 11
- 239000000427 antigen Substances 0.000 description 10
- 102000036639 antigens Human genes 0.000 description 10
- 108091007433 antigens Proteins 0.000 description 10
- 241000283973 Oryctolagus cuniculus Species 0.000 description 8
- 201000011510 cancer Diseases 0.000 description 8
- 230000036039 immunity Effects 0.000 description 7
- 238000002347 injection Methods 0.000 description 5
- 239000007924 injection Substances 0.000 description 5
- 241000699666 Mus <mouse, genus> Species 0.000 description 3
- 241000699670 Mus sp. Species 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 206010008342 Cervix carcinoma Diseases 0.000 description 2
- 240000002853 Nelumbo nucifera Species 0.000 description 2
- 235000006508 Nelumbo nucifera Nutrition 0.000 description 2
- 235000006510 Nelumbo pentapetala Nutrition 0.000 description 2
- 208000006105 Uterine Cervical Neoplasms Diseases 0.000 description 2
- 239000002671 adjuvant Substances 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 239000013592 cell lysate Substances 0.000 description 2
- 201000010881 cervical cancer Diseases 0.000 description 2
- 238000013399 early diagnosis Methods 0.000 description 2
- 210000004072 lung Anatomy 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 210000003462 vein Anatomy 0.000 description 2
- 238000001262 western blot Methods 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 208000005718 Stomach Neoplasms Diseases 0.000 description 1
- 210000005252 bulbus oculi Anatomy 0.000 description 1
- 238000005336 cracking Methods 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 235000011389 fruit/vegetable juice Nutrition 0.000 description 1
- 210000002216 heart Anatomy 0.000 description 1
- 238000003119 immunoblot Methods 0.000 description 1
- 238000009169 immunotherapy Methods 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 201000007270 liver cancer Diseases 0.000 description 1
- 208000014018 liver neoplasm Diseases 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000004570 mortar (masonry) Substances 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 201000011549 stomach cancer Diseases 0.000 description 1
- 230000005760 tumorsuppression Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/415—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Botany (AREA)
- Peptides Or Proteins (AREA)
Abstract
The invention provides a plant protein extracted from low-grade plant lichens. According to the verification, the protein is high in tumor antigenicity. The invention also discloses a method for preparing the plant protein. The plant protein can be effectively combined with cell extracts of at least seven tumor cells (human breast cancer cells, gastric carcinoma cells, pulmonary squamous carcinoma cells, human colon cancer cells, uterine cervix carcinoma cells, hepatoma carcinoma cells and human renal carcinoma cells).
Description
Technical field
The invention belongs to biological technical field, especially relate to a kind of tumor antigenicity vegetable-protein.
Background technology
Because cancer can not carry out early detection at present, and the determination of tumour antigen is significant to immunotherapy of tumors, and have been reported and find that the isoformgene of different genera shows as certain homology, biological sibship is far away, and its immunity is stronger.Accordingly, people just expect the tumor antigenicity material that can find a class xenogenesis homology, and utilize tumour antibody in its human body, realize the object of early diagnosis of cancer.
Summary of the invention
This research is extracted a kind of vegetable-protein from lower plant lichens, confirms that this kind of albumen has tumor antigenicity by immunoblotting (Westen Blotting), can as the marker of infantile tumour diagnosis.
The object of this invention is to provide a kind of tumor antigenicity vegetable-protein, be vegetable-protein by this protein designations, this vegetable-protein has tumor associated antigen.
A kind of tumor antigenicity vegetable-protein, the amino acid forming this albumen has the sequence of SEQ ID NO:1, and this albumen can be used for the detection of tumour, also can be used for the medicine preparing Tumor suppression growth.
Prepare the method for this tumor antigenicity vegetable-protein:
(6) take 40g Lichen tissue, smash to pieces, then carry out fragmentation with liquid nitrogen grinding and ultrasonic fragmentation respectively, centrifugal after broken, dissolve supernatant liquor with phosphate buffered saline buffer;
(7) with distilled water or phosphate buffered saline buffer freeze-thaw method broken further to the Lichen tissue cell obtained, centrifuging and taking supernatant after cytoclasis;
(8) ammonium sulfate precipitation is slightly carried albumen, add ammonium sulfate to 20% saturation ratio, centrifuging and taking supernatant after vulcanization acid ammonium salt to 40% saturation ratio, centrifugal, the 1mmol/L phosphoric acid buffer (ph6.8) of precipitation equivalent dissolves, and can obtain the sulfuric acid of 20%-40%, centrifugal rear on reset and add ammonium sulfate to 60% saturation ratio, centrifugal, the 1mmol/L phosphoric acid buffer (ph6.8) of precipitation equivalent dissolves, the ammonium sulfate precipitation crude protein of ammonium precipitation crude protein and 40%-60%;
(9) above-mentioned two kinds of crude protein are after Preliminary detection, by the extracting solution containing target protein after membrane filtration, carry out desalination by sephadex25 desalting column;
(10) after desalination, upper adsorptivity HA post, with the ever-increasing phosphate buffered saline buffer of ionic strength (ph6.8 is containing different concns Nacl) wash-out, Fraction collection, detects target protein in each concentration elutriant collected with SDS-PAGE protein electrophoresis;
(6) detect the concentration of the pure albumen of gained with Xylene Brilliant Cyanine G test kit ,-70 DEG C save backup.
Further, above-mentioned steps all lucifuge and not higher than the condition of 4 DEG C under carry out.
Further, centrifugal in step (2) is 4 DEG C, 5000r/min, 15min.
The pure vegetable protein extracted obtains the protein sequence of SEQ ID NO:1 through the order-checking of N end.
The application of this vegetable-protein in cancer early detection.
The application of this vegetable-protein in cancer therapy drug.
Verified, this vegetable-protein all can effectively be combined with the cytoclasis thing of human breast cancer cell, stomach cancer cell, Lung Squamous Carcinoma Cells, human colon cancer cell, cervical cancer cell, human liver cancer cell, human renal carcinoma cell, confirms that this vegetable-protein has the characteristic of kinds of tumors antigen.
Accompanying drawing explanation
Fig. 1 is the SDS-PAGE electrophorogram of this vegetable-protein.
Fig. 2 is that the western-blot that this vegetable-protein is combined with seven kinds of tumor markerses schemes.
Embodiment
The preparation of embodiment 1. vegetable protein
Take 40g Lichen tissue, mortar is smashed to pieces, then carries out fragmentation with liquid nitrogen grinding and ultrasonic fragmentation respectively, centrifugal after broken, dissolves supernatant liquor with phosphate buffered saline buffer; Carry out fragmentation to the cell of the tissue juice obtained further with phosphate buffered saline buffer freeze-thaw method, at 4 DEG C, 5000rpm, through centrifugal 15min, gets supernatant liquor; Add ammonium sulfate to 20% saturation ratio, 4 DEG C are spent the night, the centrifugal 10min of 5000rpm, in supernatant liquor, add ammonium sulfate to 40% saturation ratio, 4 DEG C are spent the night, the centrifugal 10min of 5000rpm, collecting precipitation, dissolve with 1mmol/L phosphoric acid buffer (ph6.8), dissolution precipitation, obtains 20%-40% ammonium sulfate precipitation crude protein.Continue to add ammonium sulfate to 60% saturation ratio in above-mentioned supernatant liquor, 4 DEG C are spent the night, the centrifugal 10min of 5000rpm, collecting precipitation, the 1mmol/L phosphoric acid buffer (ph6.8) of precipitation equivalent dissolves, obtain 40%-60% ammonium sulfate precipitation crude protein, the present embodiment carries out further separation and purification to 40%-60% ammonium sulfate precipitation crude protein.
By above-mentioned crude protein after filtering, desalination is carried out by the desalination of sephadex25 post.Go up adsorptivity HA post again, with the ever-increasing phosphate buffered saline buffer wash-out of ionic strength, (concentration of elutriant uses the NaCl solution wash-out of 0.05mol/L, 0.10mol/L, 0.20mol/L, 0.30mol/L, 0.40mol/L, 0.8mol/L, 1.Omol/L successively, the PH of elutriant is 6.8), Fraction collection, collect the albumen of each eluate concentration, detect the albumen of each wash-out concentration with SDS-PAGE protein electrophoresis.The elutriant containing the NaCl of 0.8mol/L after testing contains the single band of target protein, and as shown in Figure 1, the size of this vegetable-protein is 47KD, consistent with the molecular size range analyzed through bioinformatics software.
The preparation of embodiment 2. rabbit anti-plant protein antibody
The vegetable-protein prepared is prepared into injection liquid, select the Female New Zealand big white mouse of 1.5-2kg, every immunity in 3 weeks once, immunity 4 times altogether, first time immunity 0.4g antigen adds complete Freund's adjuvant and carries out immunity through dorsal sc multiple spot (being no less than 8 points) injections of antigens, three intramuscular injection 0.2g antigens next add incomplete Freund's adjuvant and carry out immunity, immunity is after 7 days the last time, blood separation of serum is got in ear vein, with tiring of indirect elisa method agreement serum antibody, tiring is 2 × 10
1.
The Western-blot of the anti-vegetable-protein of embodiment 3. rabbit and tumour antigen detects
Get seven kinds of cancer cells and be respectively MCF-7 Human Breast Cancer Cells, BGC-823 Cells, lung squamous cancer NCI-H520 cell, human colon carcinoma SW480 cell, cervical cancer Hela cell, human hepatoma HepG2 cell, people kidney HEK293 cell, seven kinds of cancer cells are carried out cracking, take cell lysate as antigen, in embodiment 2, the rabbit anti-plant protein antibody of preparation is antibody, then be combined with immune complex with mouse-anti rabbit monoclonal antibodies, combine with the sheep anti mouse polyclonal antibody of HRP mark again, then detect with ECL luminescent solution, detected result as shown in Figure 2, protein electrophoresis result shows, the seven kinds of cancer cell lysate in position of 90kD and the antibody of this vegetable-protein all have in conjunction with band, prove that rabbit resists the antibody capable of this vegetable-protein to be effectively combined with the antigen of seven kinds of cancer cells, this vegetable-protein has the characteristic of kinds of tumors antigen.
Embodiment 4. vegetable protein early diagnosis of tumor is applied
With
131i marks the rabbit anti-plant protein antibody in embodiment 2, detects its distribution in tumor-bearing mice body,
131i mark rabbit anti-plant protein antibody by its through tail vein injection to lotus S-180 transplanted tumor mouse, after injection, 12h, 24h, 36h, 48h, 72h and 96h put to death animal respectively, carry out radio-immuno-image, get a certain amount of eyeball blood, the heart, liver, spleen and tumor tissues, weigh and use γ-counter to measure its radiocounting.
Result:
131rabbit anti-plant protein antibody 36-96h tumor locus in injection Mice Body of I mark has radioactivity dense poly-, the position size of high radioactivity Nong Ju district and tumor-bearing mice institute lotus knurl is basically identical, video picture is the most clear with 48-72h after injecting antibody, the uptake ratio of each phase tumor tissues is significantly higher than other parenchymatous organs tissue, at 12h, 24h, 36h, 48h, the uptake ratio of 72h and 96h tumor tissues is respectively 1.63, 2.42, 2.92, 3.10, 2.88, 2.64, the maximum value of other substantive tissue is 0.86, the ratio prolongation in time of different tumor tissues and other tissue radiation activity is constantly increased, 48h reaches the highest, 72-96h reduces again gradually, rabbit anti-plant protein antibody energy specific binding tumour cell is described.
Above specific embodiments of the invention have been described in detail, but described content being only preferred embodiment of the present invention, can not being considered to for limiting practical range of the present invention.All equalizations done according to the present patent application scope change and improve, and all should still belong within patent covering scope of the present invention.
Claims (5)
1. a tumor antigenicity vegetable-protein, is characterized in that: the amino acid forming this albumen has the sequence of SEQ ID N0:1.
2. prepare the method for tumor antigenicity vegetable-protein described in claim 1:
(1) take 40g Lichen tissue, smash to pieces, then carry out fragmentation with liquid nitrogen grinding and ultrasonic fragmentation respectively, centrifugal after broken, dissolve supernatant liquor with phosphate buffered saline buffer;
(2) with distilled water or phosphate buffered saline buffer freeze-thaw method broken further to the Lichen tissue cell obtained, centrifuging and taking supernatant after cytoclasis;
(3) ammonium sulfate precipitation is slightly carried albumen, add ammonium sulfate to 20% saturation ratio, centrifuging and taking supernatant after vulcanization acid ammonium salt to 40% saturation ratio, centrifugal, the 1mmol/L phosphoric acid buffer (ph6.8) of precipitation equivalent dissolves, and can obtain the sulfuric acid of 20%-40%, centrifugal rear on reset and add ammonium sulfate to 60% saturation ratio, centrifugal, the 1mmol/L phosphoric acid buffer (ph6.8) of precipitation equivalent dissolves, the ammonium sulfate precipitation crude protein of ammonium precipitation crude protein and 40%-60%;
(4) above-mentioned two kinds of crude protein are after Preliminary detection, by the extracting solution containing target protein after membrane filtration, carry out desalination by sephadex25 desalting column;
(5) after desalination, upper adsorptivity HA post, with the ever-increasing phosphate buffered saline buffer of ionic strength (ph6.8 is containing different concns Nacl) wash-out, Fraction collection, detects target protein in each concentration elutriant collected with SDS-PAGE protein electrophoresis;
(6) detect the concentration of the pure albumen of gained with Xylene Brilliant Cyanine G test kit ,-70 DEG C save backup.
3. the method preparing tumor antigenicity vegetable-protein according to claim 2, is characterized in that: above-mentioned steps all lucifuge and not higher than the condition of 4 DEG C under carry out.
4. the method preparing tumor antigenicity vegetable-protein according to claim 2, is characterized in that: centrifugal in step (2) is 4 DEG C, 5000r/min, 15min.
5. vegetable-protein described in claim 1 is preparing the application in cancer therapy drug.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201510038320.0A CN104650200B (en) | 2015-01-23 | 2015-01-23 | A kind of tumor antigenicity vegetable protein |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201510038320.0A CN104650200B (en) | 2015-01-23 | 2015-01-23 | A kind of tumor antigenicity vegetable protein |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN104650200A true CN104650200A (en) | 2015-05-27 |
| CN104650200B CN104650200B (en) | 2018-05-01 |
Family
ID=53241883
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201510038320.0A Expired - Fee Related CN104650200B (en) | 2015-01-23 | 2015-01-23 | A kind of tumor antigenicity vegetable protein |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN104650200B (en) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN105907729A (en) * | 2015-05-05 | 2016-08-31 | 广东东阳光药业有限公司 | Method for preparing human papilloma virus (HPV) L1 protein virus-like particles (VLP) |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101348812A (en) * | 2007-07-19 | 2009-01-21 | 中国医学科学院放射医学研究所 | Lichenin, and preparation and use thereof |
-
2015
- 2015-01-23 CN CN201510038320.0A patent/CN104650200B/en not_active Expired - Fee Related
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101348812A (en) * | 2007-07-19 | 2009-01-21 | 中国医学科学院放射医学研究所 | Lichenin, and preparation and use thereof |
Non-Patent Citations (4)
| Title |
|---|
| ARNAB DAS，ET AL: "Murine carcinoma expressing carinoembryonic antigen-like protein is restricted by antibody against neem leaf glycoprotein", 《IMMUNOLOGY LETTERS》 * |
| KOUSTAV SARKAR，ET AL: "Neem leaf glycoprotein helps to generate carcinoembryonic antigen specific anti-tumor immune responses utilizing macrophage-mediated antigen presentation", 《VACCINE》 * |
| 丁献义，等: "131I标记的一种抗植物蛋白抗体及其片段在荷瘤小鼠体内的分布", 《河北医科大学学报》 * |
| 邓学峰，等: "一种植物蛋白的肿瘤抗原活性的研究", 《免疫学杂志》 * |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN105907729A (en) * | 2015-05-05 | 2016-08-31 | 广东东阳光药业有限公司 | Method for preparing human papilloma virus (HPV) L1 protein virus-like particles (VLP) |
| CN105907729B (en) * | 2015-05-05 | 2019-08-16 | 广东东阳光药业有限公司 | A method of preparing human mammilla tumor virus L 1 protide virus-like particle |
Also Published As
| Publication number | Publication date |
|---|---|
| CN104650200B (en) | 2018-05-01 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN101928346B (en) | Monoclonal antibody of anti-human tissue kallikrein and preparation thereof | |
| RU2019110071A (en) | METHODS FOR TREATMENT OF MALIGNANT NOMINATIONS EXPRESSING PD-L1 | |
| CN103820394B (en) | Monoclonal antibodies against morphine, produce the cell strain of this antibody, morphine detection kit and preparation method thereof | |
| JPH04503072A (en) | Immunogenic composition against gastrin peptide | |
| CN103222988B (en) | A kind of American-cockroach-extract and its preparation method and application | |
| CN102417540A (en) | Polyethylene glycol-modified integrin blocking agent HM-3 and application thereof | |
| CN102180969B (en) | Monoclonal antibody with liver cancer resisting activity and application thereof | |
| CN110655556B (en) | Preparation and method of immunoregulatory peptide | |
| CN102776152A (en) | Monoclonal antibody against BTV (bluetongue virus) VP7 protein, hybridoma cell strain capable of secreting monoclonal antibody and application of hybridoma cell strain | |
| CN103849604A (en) | Hybridoma cell strain ST03, anti-aflatoxin biosynthesis precursor ST monoclonal antibody and application thereof | |
| CN104650200A (en) | Plant protein with tumor antigenicity | |
| CN107298697B (en) | Human PD-L1 protein Y123Site phosphorylation antibody and preparation method and application thereof | |
| CN101696234B (en) | Polypeptide for resisting rheumatoid arthritis and application thereof in pharmacy | |
| CN103330952B (en) | 131i labelling anti-vegf R2 chimeric Fab and application thereof | |
| CN103919810A (en) | Method for preparing long-noded pit viper water-soluble total protein lyophilized powder | |
| CN100387709C (en) | Anti HBeAg monoclone antibody cell strain, preparation method and anti HBeAg monoclone antibody | |
| CN105693864A (en) | Tripolymer TRAIL protein and application thereof | |
| Bates et al. | Prolactin and thyrotrophin content of functional transplantable pituitary tumors | |
| CN102229654B (en) | Polypeptide resistant to rheumatoid arthritis and application of polypeptide in pharmacy | |
| CN101317857A (en) | Method for extracting goat submaxillary gland biologically active substance and application thereof | |
| Chekhonin et al. | A targeted transport of 125I-labeled monoclonal antibodies to target proteins in experimental glioma focus | |
| CN109966482A (en) | A kind of hand-foot-and-mouth disease polypeptide vaccine, vaccine injecta and its preparation method and application | |
| CN102229657B (en) | Polypeptide against rheumatoid arthritis and application thereof in pharmacy | |
| CN103342744A (en) | Angiogenesis protein and application thereof | |
| CN108323750A (en) | A kind of active constituent and its extracting method and application with liver protection |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| C06 | Publication | ||
| PB01 | Publication | ||
| C10 | Entry into substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| ASS | Succession or assignment of patent right |
Owner name: TIANJIN JIFU BIO-TECHNOLOGY CO., LTD. Free format text: FORMER OWNER: ZHENG ZHENHAI Effective date: 20150910 Free format text: FORMER OWNER: ZHENG XINWEN Effective date: 20150910 |
|
| C41 | Transfer of patent application or patent right or utility model | ||
| TA01 | Transfer of patent application right |
Effective date of registration: 20150910 Address after: Four weft road 300300 Tianjin city Dongli District No. 10 (Dongli Development Zone Kelitai incubator room 202-4) Applicant after: Tianjin Ji Fu Biological Technology Co. Ltd. Address before: Five weft road 300300 Tianjin Dongli Development Zone No. 58 city Industrial Park No. 1 Building 2 District 2 building Applicant before: Zheng Zhenhai Applicant before: Zheng Xinwen |
|
| TA01 | Transfer of patent application right |
Effective date of registration: 20180322 Address after: 050000 No. 12, No. 12, No. 1, Changan District Worker Street, Shijiazhuang, Hebei Province, 203 Applicant after: Zheng Xinwen Applicant after: Zheng Zhenhai Address before: Four weft road 300300 Tianjin city Dongli District No. 10 (Dongli Development Zone Kelitai incubator room 202-4) Applicant before: Tianjin Ji Fu Biological Technology Co. Ltd. |
|
| TA01 | Transfer of patent application right | ||
| GR01 | Patent grant | ||
| GR01 | Patent grant | ||
| CF01 | Termination of patent right due to non-payment of annual fee | ||
| CF01 | Termination of patent right due to non-payment of annual fee |
Granted publication date: 20180501 Termination date: 20200123 |