CN102043059A - Two methods for preparing immunogen and coating antigen used for detecting chloramphenicol - Google Patents
Two methods for preparing immunogen and coating antigen used for detecting chloramphenicol Download PDFInfo
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- CN102043059A CN102043059A CN2009100709549A CN200910070954A CN102043059A CN 102043059 A CN102043059 A CN 102043059A CN 2009100709549 A CN2009100709549 A CN 2009100709549A CN 200910070954 A CN200910070954 A CN 200910070954A CN 102043059 A CN102043059 A CN 102043059A
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- chloramphenicol
- hap
- coating antigen
- bsa
- haptens
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- 238000000034 method Methods 0.000 title claims abstract description 33
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 title claims abstract description 30
- 239000000427 antigen Substances 0.000 title claims abstract description 22
- 102000036639 antigens Human genes 0.000 title claims abstract description 22
- 108091007433 antigens Proteins 0.000 title claims abstract description 22
- 239000011248 coating agent Substances 0.000 title claims abstract description 21
- 238000000576 coating method Methods 0.000 title claims abstract description 21
- 229960005091 chloramphenicol Drugs 0.000 title claims abstract description 17
- 230000002163 immunogen Effects 0.000 title claims abstract description 5
- 230000008878 coupling Effects 0.000 claims abstract description 17
- 238000010168 coupling process Methods 0.000 claims abstract description 17
- 238000005859 coupling reaction Methods 0.000 claims abstract description 17
- 150000002148 esters Chemical class 0.000 claims abstract description 15
- 102000014914 Carrier Proteins Human genes 0.000 claims abstract description 13
- 108010078791 Carrier Proteins Proteins 0.000 claims abstract description 13
- 238000001514 detection method Methods 0.000 claims abstract description 12
- 238000004566 IR spectroscopy Methods 0.000 claims abstract description 5
- 108091003079 Bovine Serum Albumin Proteins 0.000 claims abstract 2
- 229940098773 bovine serum albumin Drugs 0.000 claims abstract 2
- 238000002360 preparation method Methods 0.000 claims description 11
- 238000003756 stirring Methods 0.000 claims description 9
- 102000004169 proteins and genes Human genes 0.000 claims description 8
- 108090000623 proteins and genes Proteins 0.000 claims description 8
- ZAMOUSCENKQFHK-UHFFFAOYSA-N Chlorine atom Chemical compound [Cl] ZAMOUSCENKQFHK-UHFFFAOYSA-N 0.000 claims description 7
- 239000000460 chlorine Substances 0.000 claims description 7
- 229910052801 chlorine Inorganic materials 0.000 claims description 7
- 230000002194 synthesizing effect Effects 0.000 claims description 6
- LIRCDOVJWUGTMW-ZWNOBZJWSA-N Chloramphenicol succinate Chemical compound OC(=O)CCC(=O)OC[C@@H](NC(=O)C(Cl)Cl)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 LIRCDOVJWUGTMW-ZWNOBZJWSA-N 0.000 claims description 5
- 229960004357 chloramphenicol succinate Drugs 0.000 claims description 5
- 125000003368 amide group Chemical group 0.000 claims description 4
- 238000002329 infrared spectrum Methods 0.000 claims description 4
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 claims description 4
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 claims description 3
- 238000002798 spectrophotometry method Methods 0.000 claims description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 2
- 238000010189 synthetic method Methods 0.000 claims 2
- 238000006243 chemical reaction Methods 0.000 abstract description 5
- 238000011161 development Methods 0.000 abstract description 3
- 230000008033 biological extinction Effects 0.000 abstract description 2
- 108010088751 Albumins Proteins 0.000 abstract 1
- 102000009027 Albumins Human genes 0.000 abstract 1
- 238000004458 analytical method Methods 0.000 abstract 1
- 230000015572 biosynthetic process Effects 0.000 abstract 1
- 238000006193 diazotization reaction Methods 0.000 abstract 1
- 230000001900 immune effect Effects 0.000 abstract 1
- 238000003018 immunoassay Methods 0.000 abstract 1
- 238000003786 synthesis reaction Methods 0.000 abstract 1
- 229940097572 chloromycetin Drugs 0.000 description 13
- 239000000243 solution Substances 0.000 description 11
- 238000010521 absorption reaction Methods 0.000 description 7
- 239000006228 supernatant Substances 0.000 description 6
- 241001465754 Metazoa Species 0.000 description 5
- 239000002953 phosphate buffered saline Substances 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- 238000001228 spectrum Methods 0.000 description 5
- VEXZGXHMUGYJMC-UHFFFAOYSA-N hydrochloric acid Substances Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 4
- HEMHJVSKTPXQMS-UHFFFAOYSA-M sodium hydroxide Inorganic materials [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 4
- 235000013305 food Nutrition 0.000 description 3
- 230000031700 light absorption Effects 0.000 description 3
- NLKNQRATVPKPDG-UHFFFAOYSA-M potassium iodide Chemical compound [K+].[I-] NLKNQRATVPKPDG-UHFFFAOYSA-M 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- 125000000664 diazo group Chemical group [N-]=[N+]=[*] 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 238000011156 evaluation Methods 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 238000005121 nitriding Methods 0.000 description 2
- 230000008520 organization Effects 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- 238000005303 weighing Methods 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 1
- 241000606161 Chlamydia Species 0.000 description 1
- 206010059866 Drug resistance Diseases 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 241000192125 Firmicutes Species 0.000 description 1
- 206010018723 Grey syndrome neonatal Diseases 0.000 description 1
- 206010029350 Neurotoxicity Diseases 0.000 description 1
- 241000607142 Salmonella Species 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 206010044221 Toxic encephalopathy Diseases 0.000 description 1
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 1
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 description 1
- 238000000862 absorption spectrum Methods 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 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 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000003203 everyday effect Effects 0.000 description 1
- 210000003722 extracellular fluid Anatomy 0.000 description 1
- 231100000025 genetic toxicology Toxicity 0.000 description 1
- 230000001738 genotoxic effect Effects 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 230000011132 hemopoiesis Effects 0.000 description 1
- 230000008676 import Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 244000144972 livestock Species 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 230000007135 neurotoxicity Effects 0.000 description 1
- 231100000228 neurotoxicity Toxicity 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 238000006722 reduction reaction Methods 0.000 description 1
- GOLXNESZZPUPJE-UHFFFAOYSA-N spiromesifen Chemical compound CC1=CC(C)=CC(C)=C1C(C(O1)=O)=C(OC(=O)CC(C)(C)C)C11CCCC1 GOLXNESZZPUPJE-UHFFFAOYSA-N 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 238000002211 ultraviolet spectrum Methods 0.000 description 1
- 238000009777 vacuum freeze-drying Methods 0.000 description 1
- 239000000273 veterinary drug Substances 0.000 description 1
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Abstract
Two methods for preparing immunogen and coating antigen used for fast immunoassay of chloramphenicol provide basis for development of methods for immunological rapid detection of chloramphenicol. The active ester reaction and the diazotization reaction are employed respectively to synthesize the hapten of chloramphenicol with crrier of bovine serum albumin(BSA),and oval albumin(OVA). The result is identified with UV-scanning and Infrared spectrometry(IRS) and the combination ratio is calculated. The result shows that the molar extinction coefficients of hapten with BSA, OVA by the above two methods are 164523, 49402; 372723, 44601 respectively, and are obviously greater than those of hapten and carrier protein alone. The successful synthesis is further proved by the IRS analysis. Therefore a conclusion can be reached that the antigen of chloramphenicol was successfully synthesized. The coupling ratio values of hapten to BSA and OVA by active ester reaction and diazotizition reaction are 12, 2 and 30, 1 respectively.
Description
Technical field
The present invention relates to two kinds and be used for the immunogene of chlorine detection mycin and the preparation method of coating antigen.Specifically, the present invention relates to two kinds of immunogene and coating antigen preparation methods that are used for immunology fast detecting residual chloromycetin.
Background technology
Chloromycetin all has good inhibitory effect to gram-positive bacteria and Gram-negative bacteria, and Richettsia, Chlamydia are also had inhibiting effect.Imitate high inexpensively because of it, it is clinical once to be applied to humans and animals as the medicine of bacteriosis in one period, and is widely used in animal husbandry production as feed addictive.Along with the reach of science, chloromycetin is proved to be has very big toxic and side effect to body, suppresses toxicity, genetoxic, genotoxicity, neurotoxicity, grey baby's syndrome as the marrow hemopoiesis function.Long-term in addition trace is taken in chloromycetin, not only makes Escherichia coli, salmonella etc. produce drug resistance, and can cause the imbalance of body normal flora, makes people's easy infection various diseases.In view of healthy reason, FAO (Food and Agriculture Organization of the United Nation), the World Health Organization (WHO) and the restriction of many national regulations or forbid that chloromycetin is used for food animal, the Ministry of Agriculture has deleted from 2000 chloromycetin and has been listed as banning drugs version " Chinese veterinary drug allusion quotation ".And the imported food hygienic standard of European Union is: in the import animal product, must not detect chloromycetin, its implication that " must not detect " be chloromycetin content below 1 μ g/kg, promptly content is below part per billion.European Union imposed embargo to the animal derived product that China exports to European Union in 2002, just meaned that China will lose 130,000 tons the market share in European Union market and cause more than 600,000,000 dollar economic loss.And because the ban of European Union, states such as the U.S. and Japan have shown great attention to the quality of China's outlet aquatic products.
Therefore, the use for strictness monitoring chloromycetin suppresses developing of the problems referred to above, and foundation is efficient, sensitive, economic analyzing chloramphenicol residues method is necessary.With prior art relatively, with the fast detecting that the high coupling ratio immunogen chloramphenicol and the coating antigen of this method preparation is applied to residual chloromycetin in the livestock products, the result can be more accurately, fast.Have important practical significance and high business development value.
Summary of the invention
The present invention aims to provide two kinds and is used for the immunogene of chlorine detection mycin and the preparation method of coating antigen, be used to set up immunology fast detecting residual chloromycetin easy, method provides the basis accurately and rapidly.
Two kinds are used for the immunogene of chlorine detection mycin and the preparation method of coating antigen, it is characterized in that adopting following steps:
The invention provides two kinds and be used for the immunogene of chlorine detection mycin and the preparation method of coating antigen:
(1) active ester method synthesizing chloramphenicol immunogene and coating antigen: the haptens Chloramphenicol Succinate (Hap) that will contain carboxyl with active ester method carries out coupling with carrier protein (BSA or OVA).
(2) diazotising method synthesizing chloramphenicol immunogene and coating antigen: the haptens (Hap) that will contain fragrant amido with the diazotising method carries out coupling with carrier protein.
(3) absolute content of conjugate is represented (being to contain how many mg of protein in every mL conjugate solution) with the mass concentration of protein usually in the evaluation conjugate solution of haptens-conjugate (Hap-BSA and Hap-OVA), so can be by measuring the relative content (mgmL of protein in the conjugate solution
-1) measure conjugate concentration.The principle that adopts the crosslinked ratio of determined by ultraviolet spectrophotometry is to utilize material to the relation that absorption and its concentration of light is ratio, measures respectively by the concentration of two kinds of molecules of coupling.In big molecule and micromolecular conjugate, 2 kinds of molecules all have different separately maximal ultraviolet absorption peaks, and proportional with its concentration at the absorbance (A) at corresponding maximum absorption band wavelength place; But in the ultraviolet scanning spectrum of conjugate, the spectrogram that then shows as separately is sumproperties.Simple to operate and the no specimen loss of this method.
(4) Infrared spectroscopy: will synthesize good haptens-conjugate (Hap-BSA and Hap-OVA)), haptens and carrier protein carry out the infrared spectrum detection.
Description of drawings
Fig. 1 identifies coupled product for SDS-PAGE
Fig. 2 nitriding immunogene (Hap-OVA) of attaching most importance to
Fig. 3 is active ester method immunogene (Hap-BSA)
Fig. 4 is active ester method immunogene (Hap-BSA)
Fig. 5 nitriding coating antigen (Hap-OVA) of attaching most importance to
Fig. 6 is the infared spectrum of Chloramphenicol Succinate
Fig. 7 is the infared spectrum of Chloramphenicol Succinate-BSA
Fig. 8 is the infared spectrum of Chloramphenicol Succinate-OVA
Embodiment
Embodiment one
The invention provides two kinds and be used for the immunogene of chlorine detection mycin and the preparation method of coating antigen:
(1) active ester method synthesizing chloramphenicol immunogene and coating antigen: the haptens Chloramphenicol Succinate (Hap) that will contain carboxyl with active ester method carries out coupling with carrier protein (representing that with Pro this method adopts BSA or OVA).Take by weighing Hap 0.40mmol, NHS0.40mmol, DCC 0.44mmol and be dissolved in the N of 2mL, dinethylformamide, 22 ℃ stir 5h after, centrifugal, " active ester supernatant ".Pro100mg is dissolved in 10mL 0.05molL
-1, in the phosphate buffer of pH 8 (PBS), under 4 ℃ of conditions, " the active ester supernatant " that obtains above is added dropwise in the protein solution lentamente, simultaneously vigorous stirring.The potpourri that reaction obtains slowly stirs 24h at 4 ℃, so that coupling is fully finished.Reacted solution 0.01molL
-1, the phosphate buffered saline(PBS) of pH7.4 is fully dialysed, and changes liquid every day 2 times.Extracellular fluid dialysis is carried out the scanning of UV, visible light light absorption wavelength, till the Hap characteristic absorption peak no longer occurring.Hap-Pro conjugate solution after the dialysis is carried out vacuum freeze drying, and as zooperal immunogene, Hap-OVA is as the coating antigen of immune detection with Hap-BSA.
Embodiment two
(1) diazotising method synthesizing chloramphenicol immunogene and coating antigen: the haptens (Hap) that will contain fragrant amido with the diazotising method carries out coupling with carrier protein.Take by weighing the chloromycetin haptens of 0.20mmol, be dissolved in the absolute ethyl alcohol of 700 μ L, treat that haptens dissolves fully after, use 1molL
-1Hydrochloric acid transfer pH to 1.The zinc powder that adds 0.45mmol, 80 ℃ of reduction reaction 40min, centrifugal yellow limpid transparent supernatant, cooling is the haptens that contains fragrant amido.Use 1molL L
-1Hydrochloric acid supernatant pH transferred under 1,4 ℃ of condition stir, in the supernatant that obtains, slowly drip the 0.1molL of 0.7mL
-1NaNO
2Solution continues to stir 30min, and it is blue to make starch potassium iodide paper become ash until reaction.Add 0.5mg urea again, the HNO of decomposing excessive
2, stir 30min under 4 ℃ of conditions, obtain the diazo salt 1molL of Hap
-1NaOH transfers to 8 with pH, the centrifuging and taking supernatant, put into 4 ℃ standby.The Pro of 0.002mmol is dissolved in 2mL 0.02molL
-1Among the PBS of pH 8.Stir under 4 ℃ of lucifuges, diazo salt slowly is added dropwise in the Pro solution,, drip 1molL simultaneously for stablizing of pH in the maintenance adition process
-1NaOH continues to stir and spends the night.Reacted solution 0.01molL
-1, the PBS of pH7.4 fully dialyses, and method is with (1) among the embodiment one.
(2) absolute content of conjugate is represented (being to contain how many mg of protein in every mL conjugate solution) with the mass concentration of protein usually in the evaluation conjugate solution of haptens-conjugate (Hap-BSA and Hap-OVA), so can be by measuring the relative content (mgmL of protein in the conjugate solution
-1) measure conjugate concentration.Adopt the principle of the crosslinked ratio of determined by ultraviolet spectrophotometry to be, utilize material, measure respectively by the concentration of two kinds of molecules of coupling to the relation that absorption and its concentration of light is ratio.In big molecule and micromolecular conjugate, 2 kinds of molecules all have different separately maximal ultraviolet absorption peaks, and proportional with its concentration at the absorbance (A) at corresponding maximum absorption band wavelength place; But in the ultraviolet scanning spectrum of conjugate, the spectrogram that then shows as separately is sumproperties.Simple to operate and the no specimen loss of this method.UV, visible light light absorption wavelength scanning: with haptens (Hap), carrier protein (BSA and OVA), haptens-protein conjugate (Hap-BSA and Hap-OVA) respectively with the phosphate buffer dissolving and be diluted to suitable concn, carry out the scanning of UV, visible light light absorption wavelength at 200～400nm wavelength place, observe the relation of three's UV, visible light optical absorption spectra, calculate haptens and carrier protein combine than.
(3) Infrared spectroscopy: will synthesize good haptens-conjugate (Hap-BSA and Hap-OVA)), haptens and carrier protein carry out the infrared spectrum detection.
Adopt active ester method and diazotising method,, identify coupling result and calculations incorporated ratio with ultraviolet spectrum, infrared spectrum, SDS-polyacrylamide gel electrophoresis with haptens chloromycetin and bSA (BSA) and oralbumin (OVA) coupling.UV scanning result shows that the molar extinction coefficient of OVA conjugate is respectively 1.64 * 105,49402 by the haptens and the BSA of active ester method and the development of diazotising method; 3.73 * 105,46601, significantly greater than haptens and carrier protein.The haptens and the BSA of active ester method preparation, the coupling ratio of OVA is respectively 12,2; The haptens and the BSA of the preparation of diazotising method, the coupling ratio of OVA is respectively 30,1.Infrared spectroscopy has been proved conclusively the coupling success.The SDS-polyacrylamide gel electrophoresis shows that conjugate purity is higher.
Claims (4)
1. two kinds are used for the immunogene of chlorine detection mycin and the preparation method of coating antigen, it is characterized in that adopting following steps:
(1) active ester method synthesizing chloramphenicol immunogene and coating antigen: the haptens Chloramphenicol Succinate (Hap) that will contain carboxyl with active ester method carries out coupling with carrier protein.
(2) diazotising method synthesizing chloramphenicol immunogene and coating antigen: the haptens (Hap) that will contain fragrant amido with the diazotising method carries out coupling with carrier protein.
(3) adopt the crosslinked ratio of determined by ultraviolet spectrophotometry.
(4) Infrared spectroscopy: will synthesize good haptens one conjugate (Hap-BSA and Hap-OVA)), haptens and carrier protein carry out the infrared spectrum detection, the SDS-polyacrylamide gel electrophoresis is identified coupling result and calculations incorporated ratio.
2. according to the synthetic method of described immunogen chloramphenicol of claim 1 and coating antigen, it is characterized in that adopting in the step (1) 1: 1: 1 Hap of mol ratio, NHS, DCC to be dissolved in N, in the dinethylformamide.Stir 5h at 22 ℃.
3. according to the synthetic method of described immunogen chloramphenicol of claim 1 and coating antigen, it is characterized in that the 0.20mmol Chloramphenicol Succinate is dissolved in the absolute ethyl alcohol of 700 μ L in the step (2).
4. method according to claim 1 is characterized in that the described protein of step (1) (2) is meant the conventional soluble protein (bovine serum albumin(BSA) and oralbumin) that immune carrier uses that can be used as.
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Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102353774A (en) * | 2011-06-13 | 2012-02-15 | 清华大学深圳研究生院 | Immunochromatographic test paper for detecting chloramphenicol and its preparation method |
| CN103115953A (en) * | 2013-01-28 | 2013-05-22 | 广东药学院 | Efficient capillary electrophoresis method for simultaneously detecting 11 prohibited compounds in sample |
| CN103374048A (en) * | 2012-04-26 | 2013-10-30 | 北京勤邦生物技术有限公司 | Streptomycin hapten, as well as preparation method and application thereof |
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| US5968515A (en) * | 1996-06-28 | 1999-10-19 | Thaco Research, Ltd. | Methods for the quantitative analysis of organic compounds |
| CN101526537A (en) * | 2009-01-12 | 2009-09-09 | 深圳市绿诗源生物技术有限公司 | Elisa reagent for detecting chloramphenicol and method thereof |
| CN101551391A (en) * | 2009-05-07 | 2009-10-07 | 江南大学 | Immuomagnetic bead chromatographic test strip for rapidly detecting chloromycetin and preparation method thereof |
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2009
- 2009-10-26 CN CN2009100709549A patent/CN102043059A/en active Pending
Patent Citations (3)
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|---|---|---|---|---|
| US5968515A (en) * | 1996-06-28 | 1999-10-19 | Thaco Research, Ltd. | Methods for the quantitative analysis of organic compounds |
| CN101526537A (en) * | 2009-01-12 | 2009-09-09 | 深圳市绿诗源生物技术有限公司 | Elisa reagent for detecting chloramphenicol and method thereof |
| CN101551391A (en) * | 2009-05-07 | 2009-10-07 | 江南大学 | Immuomagnetic bead chromatographic test strip for rapidly detecting chloromycetin and preparation method thereof |
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Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102353774A (en) * | 2011-06-13 | 2012-02-15 | 清华大学深圳研究生院 | Immunochromatographic test paper for detecting chloramphenicol and its preparation method |
| CN103374048A (en) * | 2012-04-26 | 2013-10-30 | 北京勤邦生物技术有限公司 | Streptomycin hapten, as well as preparation method and application thereof |
| CN103374048B (en) * | 2012-04-26 | 2016-12-14 | 北京勤邦生物技术有限公司 | Streptomycin hapten and its preparation method and application |
| CN103115953A (en) * | 2013-01-28 | 2013-05-22 | 广东药学院 | Efficient capillary electrophoresis method for simultaneously detecting 11 prohibited compounds in sample |
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Application publication date: 20110504 |