CN114539360A - Moose source characteristic polypeptide and application thereof - Google Patents
Moose source characteristic polypeptide and application thereof Download PDFInfo
- Publication number
- CN114539360A CN114539360A CN202210296222.7A CN202210296222A CN114539360A CN 114539360 A CN114539360 A CN 114539360A CN 202210296222 A CN202210296222 A CN 202210296222A CN 114539360 A CN114539360 A CN 114539360A
- Authority
- CN
- China
- Prior art keywords
- solution
- moose
- sample
- deer
- mass spectrum
- 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
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N30/00—Investigating or analysing materials by separation into components using adsorption, absorption or similar phenomena or using ion-exchange, e.g. chromatography or field flow fractionation
- G01N30/02—Column chromatography
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N30/00—Investigating or analysing materials by separation into components using adsorption, absorption or similar phenomena or using ion-exchange, e.g. chromatography or field flow fractionation
- G01N30/02—Column chromatography
- G01N30/04—Preparation or injection of sample to be analysed
- G01N30/06—Preparation
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N30/00—Investigating or analysing materials by separation into components using adsorption, absorption or similar phenomena or using ion-exchange, e.g. chromatography or field flow fractionation
- G01N30/02—Column chromatography
- G01N30/26—Conditioning of the fluid carrier; Flow patterns
- G01N30/28—Control of physical parameters of the fluid carrier
- G01N30/34—Control of physical parameters of the fluid carrier of fluid composition, e.g. gradient
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N30/00—Investigating or analysing materials by separation into components using adsorption, absorption or similar phenomena or using ion-exchange, e.g. chromatography or field flow fractionation
- G01N30/02—Column chromatography
- G01N30/62—Detectors specially adapted therefor
- G01N30/72—Mass spectrometers
-
- 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
- G01N33/6803—General methods of protein analysis not limited to specific proteins or families of proteins
- G01N33/6848—Methods of protein analysis involving mass spectrometry
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N30/00—Investigating or analysing materials by separation into components using adsorption, absorption or similar phenomena or using ion-exchange, e.g. chromatography or field flow fractionation
- G01N30/02—Column chromatography
- G01N30/04—Preparation or injection of sample to be analysed
- G01N30/06—Preparation
- G01N2030/067—Preparation by reaction, e.g. derivatising the sample
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Physics & Mathematics (AREA)
- Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Immunology (AREA)
- Molecular Biology (AREA)
- Organic Chemistry (AREA)
- Pathology (AREA)
- General Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Microbiology (AREA)
- Biomedical Technology (AREA)
- Medicinal Chemistry (AREA)
- Biotechnology (AREA)
- Urology & Nephrology (AREA)
- Hematology (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Bioinformatics & Computational Biology (AREA)
- Spectroscopy & Molecular Physics (AREA)
- General Engineering & Computer Science (AREA)
- Cell Biology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Food Science & Technology (AREA)
- Other Investigation Or Analysis Of Materials By Electrical Means (AREA)
Abstract
The invention belongs to the technical field of biology, and particularly relates to a characteristic polypeptide for identifying moose and application thereof. The characteristic polypeptide provided by the invention is specifically as follows: peptide fragment 1 is shown in SEQ ID No. 1: EFTPELQADYQK are provided. The characteristic polypeptide provided by the invention has excellent specificity and stability aiming at the moose, has strong specificity, can be used for identifying adulterated moose or counterfeit products of pilose antler, deer horn medicinal materials and decoction pieces, deer skin, deer blood, deer penis and deer sinew of the moose, and has good application prospect.
Description
Technical Field
The invention belongs to the technical field of biology, and particularly relates to a characteristic polypeptide for identifying moose and application thereof.
Background
Moose is the largest cervidae animal in the world. The Cervidae animal has high economic value, and its derivative products include cornu Cervi Pantotrichum, cornu Cervi, corium Cervi, penis et testis Cervi, Carnis Cervi, sanguis Cervi, ligamentum Cervi, etc. However, the products of the torpedo dragons in the market are mixed, so that people with sheep heads hanging to sell dog meat often forge sika deer or red deer to sell by using the products of moose deer. Especially, because the moose is the biggest deer in the world, the output is large and easy to obtain, and compared with the spotted deer antler and the cervus elaphus linnaeus which are in shortage of resources, the cost is low. The deerskin, penis cervi, venison, deer blood, deer sinew and the like have similar appearances and almost the same main components, so the species cannot be distinguished by the existing identification method.
Disclosure of Invention
Aiming at the technical blank in the prior art, the invention provides a characteristic polypeptide for identifying a moose source.
The invention also provides application of the characteristic polypeptide in identifying species of moose.
The technical scheme adopted by the invention for realizing the purpose is as follows:
the invention provides a characteristic polypeptide for identifying a moose deer source, which specifically comprises the following components: peptide fragment 1 is shown in SEQ ID No. 1: EFTPELQADYQK are provided.
The characteristic polypeptide found by the invention exists in camel deer blood beta globin.
Further, the mass-to-charge ratio of the peptide segment 1 of SEQ ID No.1 is 734.85(z = 2).
The invention also provides a kit for identifying sources of moose, comprising a polypeptide according to the characteristics of claim 1.
The invention also provides a method for identifying moose source by using the characteristic polypeptide, which comprises the following steps:
(1) pretreating a sample to be detected to obtain a solution to be detected;
(2) and (3) detecting the solution to be detected by a liquid-triple quadrupole mass spectrometry, analyzing and comparing a mass spectrum result in the solution to be detected with a mass spectrum of the peptide segment 1, and judging that the sample to be detected is the moose or the adulterated moose when the mass spectrum of the peptide segment 1 appears in the mass spectrum.
Further, the pretreatment of the sample to be detected comprises the following specific processes: crushing a sample, weighing 50mg of the sample, adding 10ml of modified buffer solution and 1ml of DTT solution, shaking up, treating at 80 ℃ overnight, taking out, cooling to room temperature, centrifuging, measuring 500 mu L of supernatant, adding 100 mu L of IAA solution, reacting for 30min in a dark place, mixing uniformly, and centrifuging; desalting the sample solution, measuring supernatant 100 μ L, adding 900 μ L ammonium bicarbonate solution (1%) and 10 μ L bovine trypsin solution, performing enzymolysis at 37 deg.C for 4 hr, taking out, cooling to room temperature, centrifuging, and collecting supernatant.
The specific preparation process of the denaturation buffer solution comprises the following steps: weighing 573.1g of guanidine hydrochloride, 121.1g of tris (hydroxymethyl) aminomethane and 0.734g of ethylenediamine tetraacetic acid, adding water for dissolving, adding concentrated hydrochloric acid for adjusting the pH value to 8.0, adding water for diluting to 1L, and shaking up to obtain the product; the concentration of the DTT solution is 2.5M; the IAA solution was at a concentration of 2M.
Further, the specific preparation process of the bovine trypsin solution comprises the following steps: weighing a proper amount of bovine trypsin, dissolving with an acetic acid solution to prepare a solution with the concentration of 10mg/ml, and preparing the solution immediately after use; the concentration of the acetic acid solution was 2%.
In the liquid phase-triple quadrupole mass spectrometry, the liquid phase conditions are as follows: the chromatographic column was ACQUITY UPLC BEH C18 (2.1X 50mm, 1.7 μm), the column temperature was 43 ℃, the flow rate was 0.3mL/min, the mobile phase A was 0.1% formic acid solution, the B was 0.1% formic acid acetonitrile solution, and gradient elution was performed.
The conditions for the gradient elution are as follows: 0-9 min,3% B → 7.5% B; 9-13 min, 7.5% B → 25% B; 13-14 min,25% B → 90% B; 14-17 min, 90% B; 17-17.5 min, 10% B-97% B; 17.5-21 min,97% B, and the sample injection amount is 5 mu L.
In the liquid phase-triple quadrupole mass spectrometry used in the present invention, mass spectrometry conditions are as follows: performing multi-reaction monitoring in a positive ion mode by adopting a mass spectrum detector and electrospray ionization (ESI); sheath gas flow rate 46L/hr; auxiliary gas flow rate 850L/hr; the spraying voltage is 3.5 KV; the ion source temperature is 150 ℃; the temperature of the auxiliary gas is 400 ℃; a taper hole voltage of 30V and a collision voltage of 35V); the solvent delay (solvent delay) is 0-8 min and 14-20 min; m/z (two charges) 734.85 → 249.10, 734.85 → 360.20 are selected as the detecting ion pair.
The invention has the beneficial effects that:
(1) the characteristic polypeptide and the detection method provided by the invention provide a solution for the inspection of products mixed with the moose or using the moose to replace sika deer and red deer.
(2) The characteristic polypeptide provided by the invention has excellent specificity and stability, strong specificity and good application prospect aiming at pilose antler, deer horn, deer skin, deer penis, deer meat, deer blood, deer sinew and the like.
Drawings
FIG. 1 shows the secondary mass spectrum of m/z (two charges) 734.85 and the assignment of y and b ions.
FIG. 2 shows the results of a proprietary experiment for m/z (two charges) 734.85.
FIG. 3 shows the BLAST (basic Local Alignment Search tool) results of EFTPELQADYQK.
Detailed Description
The technical solution of the present invention is further explained and illustrated by the following specific embodiments.
Instrument and reagent: thermo EASY-nLC 1000 nanoliter liquid phase, Thermo Scientific Orbitrap-Fusion high resolution mass spectrum, AB Triple Quad 6500+ HPLC mass spectrometer, Sidoristes XSE205 electronic balance, trypsin (Sigma, batch: SLBG 6452V) guanidine hydrochloride, Tris (hydroxymethyl) aminomethane (Tris), Ethylene Diamine Tetraacetic Acid (EDTA), Dithiothreitol (DTT), Iodoacetamide (IAA), ammonium bicarbonate, acetic acid are all analytically pure. Formic acid and acetonitrile are both chromatographically pure.
The deer source is verified by PCR experiments of Shandong province agricultural academy of sciences, provided by enterprises.
Example 1
1. Measurement conditions
1.1 liquid phase-triple quadrupole mass spectrometry conditions
Liquid phase conditions: the chromatographic column was ACQUITY UPLC BEH C18 (2.1X 50mm, 1.7 μm), the column temperature was 43 ℃, the flow rate was 0.3mL/min, the mobile phase A was 0.1% formic acid solution, the B was 0.1% formic acid acetonitrile solution, and gradient elution was performed. (0-9 min,3% B → 7.5% B; 9-13 min, 7.5% B → 25% B; 13-14 min,25% B → 90% B; 14-17 min, 90% B; 17-17.5 min, 10% B-97% B; 17.5-21 min,97% B) the amount of the sample to be sampled was 5. Mass spectrum conditions: performing multi-reaction monitoring in a positive ion mode by adopting a mass spectrum detector and electrospray ionization (ESI); sheath gas flow rate 46L/hr; auxiliary gas flow rate 850L/hr; the spraying voltage is 3.5 KV; the ion source temperature is 150 ℃; the temperature of the auxiliary gas is 400 ℃. Cone voltage 30V, impact voltage 35V). The solvent delay (solvent delay) is 0-8 min and 14-20 min. M/z (two charges) 734.85 → 249.10, 734.85 → 360.20 are selected as the detecting ion pair.
Preparation of test solution
Sample preparation: the determination was performed using a sample of velvet antler. Firstly, crushing a sample, weighing 50mg of the sample, adding 10ml of a denaturation buffer solution (weighing 573.1g of guanidine hydrochloride, 121.1g of tris (hydroxymethyl) aminomethane and 0.734g of ethylenediamine tetraacetic acid, adding water to dissolve, adding concentrated hydrochloric acid to adjust the pH value to 8.0, adding water to dilute to 1L, and shaking up to obtain the reagent). And 1ml of DTT solution, shaken well, treated overnight at 80 ℃, taken out, cooled to room temperature, and centrifuged (12000 rpm, 10 min). Weighing 500 μ L of supernatant, adding 100 μ L of IAA solution, reacting for 30min in dark place, mixing, and centrifuging (12000 rpm, 10 min); desalting the sample solution, measuring supernatant 100 μ L, adding 900 μ L ammonium bicarbonate solution (1%) and 10 μ L bovine trypsin solution (weighing appropriate amount of bovine trypsin, dissolving with acetic acid solution to obtain 10mg/ml solution, mixing immediately), performing enzymolysis at 37 deg.C for 4 hr, cooling to room temperature, centrifuging (12000 rpm, 10 min), and collecting supernatant. The results are shown in Table 1, and the picture of the results is shown in FIG. 1.
TABLE 1 results of the specificity experiments
The characteristic peptide segment is attributed to beta globin in deer blood, so the characteristic peptide segment can be applied to identifying deer products with rich blood content, such as camel antler, deer skin, deer penis, deer meat, deer blood, deer sinew and the like.
Comparative example 1
When the deer antler samples were measured using ion pairs (m/z)553.29 (two charges) → 285.16 (m/z)553.29 (two charges) → 329.19, which were previously searched for in the subject group, it was found that, in addition to the absorption peaks of the moose, the red deer also showed absorption peaks in the sika deer.
<110> Shandong province food and drug inspection research institute
<120> moose source characteristic polypeptide and application thereof
<160> 1
<210> 1
<211>15
<212>PRT
<222>（1）…（12）
<400>1
Glu Phe Thr Pro Glu Leu Gln Ala Asp Tyr Gln Lys
1 5 10
Claims (10)
1. A characteristic polypeptide for identifying moose deer is characterized in that the characteristic polypeptide specifically comprises: peptide fragment 1 is shown in SEQ ID No. 1: EFTPELQADYQK are provided.
2. The signature polypeptide of claim 1, wherein the mass-to-charge ratio of peptide stretch 1 of SEQ ID No.1 is 734.85(z = 2).
3. A kit for identifying a moose, comprising the signature polypeptide of claim 1.
4. A method for identifying elk using the signature polypeptide of claim 1 or 2, comprising the steps of:
(1) pretreating a sample to be detected to obtain a solution to be detected;
(2) and detecting the solution to be detected by a liquid-triple quadrupole mass spectrometry, analyzing and comparing a mass spectrum result in the solution to be detected with a mass spectrum of the peptide fragment 1, and judging that the sample to be detected contains the moose source component when the mass spectrum of the peptide fragment 1 appears in the mass spectrum.
5. The method according to claim 4, wherein the pre-treatment of the sample to be tested comprises the following specific steps: crushing a sample, weighing 50mg of the sample, adding 10ml of modified buffer solution and 1ml of DTT solution, shaking up, standing at 80 ℃ for overnight treatment, taking out, cooling to room temperature, centrifuging, measuring 500 mu L of supernate, adding 100 mu L of IAA solution, reacting for 30min in a dark place, mixing uniformly, and centrifuging; desalting the sample solution, measuring supernatant 100 μ L, adding 900 μ L ammonium bicarbonate solution (1%) and 10 μ L bovine trypsin solution, performing enzymolysis at 37 deg.C for 4 hr, taking out, cooling to room temperature, centrifuging, and collecting supernatant.
6. The method according to claim 5, wherein the denaturing buffer is prepared by the following steps: weighing 573.1g of guanidine hydrochloride, 121.1g of tris (hydroxymethyl) aminomethane and 0.734g of ethylenediamine tetraacetic acid, adding water for dissolving, adding concentrated hydrochloric acid for adjusting the pH value to 8.0, adding water for diluting to 1L, and shaking up to obtain the product; the concentration of the DTT solution is 2.5M; the IAA solution was at a concentration of 2M.
7. The method according to claim 5 or 6, wherein the bovine trypsin solution is prepared by the following specific steps: weighing a proper amount of bovine trypsin, dissolving with an acetic acid solution to prepare a solution with the concentration of 10mg/ml, and preparing the solution on site; the concentration of the acetic acid solution was 2%.
8. The method of any one of claims 4 to 7, wherein in the liquid phase-triple quadrupole mass spectrometry, the liquid phase conditions are: the chromatographic column is ACQUITY UPLC BEH C18 (2.1X 50mm, 1.7 mu m), the column temperature is 43 ℃, the flow rate is 0.3mL/min, the mobile phase A is 0.1 percent formic acid solution, the B is 0.1 percent formic acid acetonitrile solution, and gradient elution is carried out.
9. The method of claim 8, wherein the conditions of the gradient elution are: 0-9 min,3% B → 7.5% B; 9-13 min, 7.5% B → 25% B; 13-14 min,25% B → 90% B; 14-17 min, 90% B; 17-17.5 min, 10% B-97% B; 17.5-21 min,97% B, and the sample injection amount is 5 mul.
10. The method of claim 8 or 9, wherein in the liquid-triple quadrupole mass spectrometry, the mass spectrometry conditions are: performing multi-reaction monitoring in a mass spectrum detector, electrospray ionization (ESI) and positive ion mode; sheath gas flow rate 46L/hr; auxiliary gas flow rate 850L/hr; the spraying voltage is 3.5 KV; the ion source temperature is 150 ℃; the temperature of the auxiliary gas is 400 ℃; a taper hole voltage of 30V and a collision voltage of 35V); the solvent delay (solvent delay) is 0-8 min and 14-20 min; m/z (two charges) 734.85 → 249.10, 734.85 → 360.20 are selected as the detecting ion pair.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202210296222.7A CN114539360B (en) | 2022-03-24 | 2022-03-24 | Polypeptide with characteristics of elk source and application thereof |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN202210296222.7A CN114539360B (en) | 2022-03-24 | 2022-03-24 | Polypeptide with characteristics of elk source and application thereof |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN114539360A true CN114539360A (en) | 2022-05-27 |
| CN114539360B CN114539360B (en) | 2023-04-28 |
Family
ID=81665210
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN202210296222.7A Active CN114539360B (en) | 2022-03-24 | 2022-03-24 | Polypeptide with characteristics of elk source and application thereof |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN114539360B (en) |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN115925789A (en) * | 2022-06-02 | 2023-04-07 | 山东省食品药品检验研究院 | Characteristic polypeptide library for identifying species source of deer product mixture and application thereof |
| CN116143874A (en) * | 2022-06-01 | 2023-05-23 | 山东省食品药品检验研究院 | Polypeptide for identifying sika deer or red deer source characteristics and application thereof |
| CN116284247A (en) * | 2023-01-06 | 2023-06-23 | 山东省食品药品检验研究院 | Characteristic polypeptide for identifying deerhorn glue confusion product, and combination method and application thereof |
| JP7400139B1 (en) | 2022-06-02 | 2023-12-18 | 山東省食品薬品検験研究院 | Characteristic polypeptide library and its use for rapid differentiation of antler species and genera |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN112098579A (en) * | 2020-09-01 | 2020-12-18 | 南京中医药大学 | Deer-derived characteristic peptide fragment and detection method thereof |
| CN112898384A (en) * | 2021-01-23 | 2021-06-04 | 南京中医药大学 | Deer horn characteristic peptide segment and detection method thereof |
| CN113307846A (en) * | 2021-06-23 | 2021-08-27 | 山东省食品药品检验研究院 | Characteristic polypeptide for identifying deer antlers of sika deer or red deer and application thereof |
| CN113480599A (en) * | 2021-06-23 | 2021-10-08 | 山东省食品药品检验研究院 | Characteristic polypeptide for identifying deer antler glue of sika deer or red deer and application thereof |
-
2022
- 2022-03-24 CN CN202210296222.7A patent/CN114539360B/en active Active
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN112098579A (en) * | 2020-09-01 | 2020-12-18 | 南京中医药大学 | Deer-derived characteristic peptide fragment and detection method thereof |
| CN112898384A (en) * | 2021-01-23 | 2021-06-04 | 南京中医药大学 | Deer horn characteristic peptide segment and detection method thereof |
| CN113307846A (en) * | 2021-06-23 | 2021-08-27 | 山东省食品药品检验研究院 | Characteristic polypeptide for identifying deer antlers of sika deer or red deer and application thereof |
| CN113480599A (en) * | 2021-06-23 | 2021-10-08 | 山东省食品药品检验研究院 | Characteristic polypeptide for identifying deer antler glue of sika deer or red deer and application thereof |
Non-Patent Citations (1)
| Title |
|---|
| 无: "HBB_ALCAA", 《NCBI》 * |
Cited By (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN116143874A (en) * | 2022-06-01 | 2023-05-23 | 山东省食品药品检验研究院 | Polypeptide for identifying sika deer or red deer source characteristics and application thereof |
| CN116143874B (en) * | 2022-06-01 | 2023-09-26 | 山东省食品药品检验研究院 | Polypeptide for identifying sika deer or red deer source characteristics and application thereof |
| CN115925789A (en) * | 2022-06-02 | 2023-04-07 | 山东省食品药品检验研究院 | Characteristic polypeptide library for identifying species source of deer product mixture and application thereof |
| CN115925789B (en) * | 2022-06-02 | 2023-06-23 | 山东省食品药品检验研究院 | Characteristic polypeptide library for identifying deer product mixture genus source and application thereof |
| JP7400139B1 (en) | 2022-06-02 | 2023-12-18 | 山東省食品薬品検験研究院 | Characteristic polypeptide library and its use for rapid differentiation of antler species and genera |
| CN116284247A (en) * | 2023-01-06 | 2023-06-23 | 山东省食品药品检验研究院 | Characteristic polypeptide for identifying deerhorn glue confusion product, and combination method and application thereof |
| CN116284247B (en) * | 2023-01-06 | 2023-10-03 | 山东省食品药品检验研究院 | Characteristic polypeptide for identifying deerhorn glue confusion product, and combination method and application thereof |
Also Published As
| Publication number | Publication date |
|---|---|
| CN114539360B (en) | 2023-04-28 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN114539360B (en) | Polypeptide with characteristics of elk source and application thereof | |
| CN113307846A (en) | Characteristic polypeptide for identifying deer antlers of sika deer or red deer and application thereof | |
| CN113480599A (en) | Characteristic polypeptide for identifying deer antler glue of sika deer or red deer and application thereof | |
| Beavis et al. | Rapid, sensitive analysis of protein mixtures by mass spectrometry. | |
| Chua et al. | Honey protein extraction and determination by mass spectrometry | |
| CN104797939B (en) | The apparatus and method of microbiological analysis | |
| CN114591421B (en) | Characteristic polypeptide for identifying reindeer source and application thereof | |
| Encinar et al. | Methodological advances for selenium speciation analysis in yeast | |
| Gu et al. | A rapid solid-phase extraction combined with liquid chromatography-tandem mass spectrometry for simultaneous screening of multiple allergens in chocolates | |
| CN110596262A (en) | Method for measuring content of Apis cerana MRJP1 protein in honey by using liquid chromatography tandem mass spectrometry | |
| Yu et al. | Doping control analysis of recombinant human erythropoietin, darbepoetin alfa and methoxy polyethylene glycol-epoetin beta in equine plasma by nano-liquid chromatography–tandem mass spectrometry | |
| CN106589063B (en) | Donkey-derived characteristic peptides and application process thereof in qualitative detection of donkey skin and donkey-hide gelatin | |
| CN106855543A (en) | A kind of protein isotopic dilution tandem mass spectrum detection method based on chemical labeling techniques | |
| CN116284247A (en) | Characteristic polypeptide for identifying deerhorn glue confusion product, and combination method and application thereof | |
| Wenner et al. | Factors that affect ion trap data-dependent MS/MS in proteomics | |
| Muccilli et al. | Characterisation of a specific class of typical low molecular weight glutenin subunits of durum wheat by a proteomic approach | |
| Caldas et al. | Electrospray ionization mass spectrometry of sphinganine analog mycotoxins | |
| CN110850002A (en) | Method for quantifying honey MRJP2 in liquid chromatography tandem mass spectrometry | |
| CN111060696A (en) | Method for reducing false positive rate of plant small molecule signal peptide | |
| Ojima et al. | Droplet electrocoupling between capillary electrophoresis and matrix assisted laser desorption/ionization‐time of flight‐mass spectroscopy and its application | |
| Ruhland et al. | Food fraud: A simple and efficient LC–MS/MS approach for peptide-based food authentication | |
| Preston et al. | Isotope dilution analysis of combined nitrogen in natural waters: II. amino acids | |
| Fang-Jie et al. | High concentration trypsin assisted fast in-gel digestion for phosphoproteome analysis | |
| CN111579705B (en) | Jujube flower honey authenticity evaluation method and application | |
| CN114591399B (en) | Characteristic polypeptide for screening reindeer antler feed material in traditional Chinese medicine preparation and application thereof |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| PB01 | Publication | ||
| PB01 | Publication | ||
| SE01 | Entry into force of request for substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| GR01 | Patent grant | ||
| GR01 | Patent grant |