CN111157465A - α -amylase detection method - Google Patents
α -amylase detection method Download PDFInfo
- Publication number
- CN111157465A CN111157465A CN201911392244.8A CN201911392244A CN111157465A CN 111157465 A CN111157465 A CN 111157465A CN 201911392244 A CN201911392244 A CN 201911392244A CN 111157465 A CN111157465 A CN 111157465A
- Authority
- CN
- China
- Prior art keywords
- amylase
- detecting
- detected
- sample
- sodium
- 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.)
- Pending
Links
- 238000001514 detection method Methods 0.000 title claims abstract description 26
- 102000004139 alpha-Amylases Human genes 0.000 title claims abstract description 23
- 108090000637 alpha-Amylases Proteins 0.000 title claims abstract description 23
- 229940024171 alpha-amylase Drugs 0.000 title claims abstract description 23
- 210000002966 serum Anatomy 0.000 claims abstract description 21
- NALMPLUMOWIVJC-UHFFFAOYSA-N n,n,4-trimethylbenzeneamine oxide Chemical compound CC1=CC=C([N+](C)(C)[O-])C=C1 NALMPLUMOWIVJC-UHFFFAOYSA-N 0.000 claims abstract description 15
- 239000011697 sodium iodate Substances 0.000 claims abstract description 15
- 229940032753 sodium iodate Drugs 0.000 claims abstract description 15
- 235000015281 sodium iodate Nutrition 0.000 claims abstract description 15
- 238000005119 centrifugation Methods 0.000 claims abstract description 13
- 239000006228 supernatant Substances 0.000 claims abstract description 13
- DWAQJAXMDSEUJJ-UHFFFAOYSA-M Sodium bisulfite Chemical compound [Na+].OS([O-])=O DWAQJAXMDSEUJJ-UHFFFAOYSA-M 0.000 claims abstract description 12
- 229920002472 Starch Polymers 0.000 claims abstract description 12
- 235000010267 sodium hydrogen sulphite Nutrition 0.000 claims abstract description 12
- 235000019698 starch Nutrition 0.000 claims abstract description 12
- 239000008107 starch Substances 0.000 claims abstract description 12
- 238000002835 absorbance Methods 0.000 claims abstract description 10
- 238000006243 chemical reaction Methods 0.000 claims abstract description 8
- 239000007853 buffer solution Substances 0.000 claims abstract description 5
- 238000000034 method Methods 0.000 claims description 24
- 206010018910 Haemolysis Diseases 0.000 claims description 9
- 230000008588 hemolysis Effects 0.000 claims description 9
- 239000008055 phosphate buffer solution Substances 0.000 claims description 8
- 239000008363 phosphate buffer Substances 0.000 claims description 7
- 239000000243 solution Substances 0.000 claims description 6
- LEAHFJQFYSDGGP-UHFFFAOYSA-K trisodium;dihydrogen phosphate;hydrogen phosphate Chemical group [Na+].[Na+].[Na+].OP(O)([O-])=O.OP([O-])([O-])=O LEAHFJQFYSDGGP-UHFFFAOYSA-K 0.000 claims description 6
- 108010019160 Pancreatin Proteins 0.000 claims description 3
- 229940055695 pancreatin Drugs 0.000 claims description 3
- 239000000843 powder Substances 0.000 claims description 3
- 230000002949 hemolytic effect Effects 0.000 abstract description 6
- 239000007788 liquid Substances 0.000 abstract description 4
- 210000004369 blood Anatomy 0.000 description 6
- 239000008280 blood Substances 0.000 description 6
- NLKNQRATVPKPDG-UHFFFAOYSA-M potassium iodide Chemical compound [K+].[I-] NLKNQRATVPKPDG-UHFFFAOYSA-M 0.000 description 6
- 206010033645 Pancreatitis Diseases 0.000 description 5
- 206010033647 Pancreatitis acute Diseases 0.000 description 5
- 201000003229 acute pancreatitis Diseases 0.000 description 5
- 239000004382 Amylase Substances 0.000 description 4
- 102000013142 Amylases Human genes 0.000 description 4
- 108010065511 Amylases Proteins 0.000 description 4
- BPYKTIZUTYGOLE-IFADSCNNSA-N Bilirubin Chemical compound N1C(=O)C(C)=C(C=C)\C1=C\C1=C(C)C(CCC(O)=O)=C(CC2=C(C(C)=C(\C=C/3C(=C(C=C)C(=O)N\3)C)N2)CCC(O)=O)N1 BPYKTIZUTYGOLE-IFADSCNNSA-N 0.000 description 4
- 235000019418 amylase Nutrition 0.000 description 4
- 238000011161 development Methods 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- ZCYVEMRRCGMTRW-UHFFFAOYSA-N 7553-56-2 Chemical compound [I] ZCYVEMRRCGMTRW-UHFFFAOYSA-N 0.000 description 2
- 229910052740 iodine Inorganic materials 0.000 description 2
- 239000011630 iodine Substances 0.000 description 2
- 230000035484 reaction time Effects 0.000 description 2
- 238000011895 specific detection Methods 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 230000002485 urinary effect Effects 0.000 description 2
- 210000002700 urine Anatomy 0.000 description 2
- 206010003011 Appendicitis Diseases 0.000 description 1
- 208000005647 Mumps Diseases 0.000 description 1
- 206010061902 Pancreatic neoplasm Diseases 0.000 description 1
- 208000025865 Ulcer Diseases 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 201000001883 cholelithiasis Diseases 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 150000003278 haem Chemical class 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 208000003243 intestinal obstruction Diseases 0.000 description 1
- PNDPGZBMCMUPRI-UHFFFAOYSA-N iodine Chemical compound II PNDPGZBMCMUPRI-UHFFFAOYSA-N 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 208000019423 liver disease Diseases 0.000 description 1
- 208000015486 malignant pancreatic neoplasm Diseases 0.000 description 1
- 239000011259 mixed solution Substances 0.000 description 1
- 229940068938 morphine injection Drugs 0.000 description 1
- 208000010805 mumps infectious disease Diseases 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 201000002528 pancreatic cancer Diseases 0.000 description 1
- 208000008443 pancreatic carcinoma Diseases 0.000 description 1
- 230000008085 renal dysfunction Effects 0.000 description 1
- 210000003079 salivary gland Anatomy 0.000 description 1
- 238000012956 testing procedure Methods 0.000 description 1
- 231100000397 ulcer Toxicity 0.000 description 1
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N21/00—Investigating or analysing materials by the use of optical means, i.e. using sub-millimetre waves, infrared, visible or ultraviolet light
- G01N21/17—Systems in which incident light is modified in accordance with the properties of the material investigated
- G01N21/25—Colour; Spectral properties, i.e. comparison of effect of material on the light at two or more different wavelengths or wavelength bands
- G01N21/31—Investigating relative effect of material at wavelengths characteristic of specific elements or molecules, e.g. atomic absorption spectrometry
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N1/00—Sampling; Preparing specimens for investigation
- G01N1/28—Preparing specimens for investigation including physical details of (bio-)chemical methods covered elsewhere, e.g. G01N33/50, C12Q
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N1/00—Sampling; Preparing specimens for investigation
- G01N1/28—Preparing specimens for investigation including physical details of (bio-)chemical methods covered elsewhere, e.g. G01N33/50, C12Q
- G01N1/286—Preparing specimens for investigation including physical details of (bio-)chemical methods covered elsewhere, e.g. G01N33/50, C12Q involving mechanical work, e.g. chopping, disintegrating, compacting, homogenising
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N21/00—Investigating or analysing materials by the use of optical means, i.e. using sub-millimetre waves, infrared, visible or ultraviolet light
- G01N21/75—Systems in which material is subjected to a chemical reaction, the progress or the result of the reaction being investigated
- G01N21/77—Systems in which material is subjected to a chemical reaction, the progress or the result of the reaction being investigated by observing the effect on a chemical indicator
- G01N21/78—Systems in which material is subjected to a chemical reaction, the progress or the result of the reaction being investigated by observing the effect on a chemical indicator producing a change of colour
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N1/00—Sampling; Preparing specimens for investigation
- G01N1/28—Preparing specimens for investigation including physical details of (bio-)chemical methods covered elsewhere, e.g. G01N33/50, C12Q
- G01N1/2813—Producing thin layers of samples on a substrate, e.g. smearing, spinning-on
- G01N2001/2846—Cytocentrifuge method
Landscapes
- Physics & Mathematics (AREA)
- Chemical & Material Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Analytical Chemistry (AREA)
- Biochemistry (AREA)
- Health & Medical Sciences (AREA)
- General Physics & Mathematics (AREA)
- Immunology (AREA)
- Pathology (AREA)
- Spectroscopy & Molecular Physics (AREA)
- Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Plasma & Fusion (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Abstract
The invention belongs to the technical field of biological detection, and particularly relates to a α -amylase detection method which comprises the following steps of S1, centrifuging a hemolytic sample to be detected, sucking out serum after centrifugation, S2, centrifuging the serum at a high speed, sucking out supernatant, S3, mixing the supernatant with soluble starch in a buffer solution to obtain a liquid to be detected, S4, mixing the liquid to be detected with sodium iodate and sodium bisulfite for reaction, detecting absorbance at a wavelength of 630nm, and calculating the concentration of α -amylase in the hemolytic sample to be detected according to the absorbance.
Description
Technical Field
The invention belongs to the technical field of biological detection, and particularly relates to a detection method of α -amylase.
Background
α -Amylase (AMY) is mainly secreted by salivary gland and pancreas, mumps, especially AMY activity in blood and urine is increased remarkably when acute pancreatitis occurs, serum AMY begins to rise 8-12 hours after acute pancreatitis occurs, the peak is reached 12-24 hours, 2-5 days are reduced to normal level, if AMY exceeds 500U, diagnosis significance is achieved, 350U is suspected to be acute pancreatitis, acute appendicitis, intestinal obstruction, pancreatic cancer, cholelithiasis, ulcer perforation and AMY after morphine injection can be increased (but is lower than 500U), AMY in serum of normal human is mainly produced by liver and gall, thus AMY in serum and urine is reduced to liver disease at the same time.
Amylase has a relative molecular weight of 50000 and can be filtered out through glomeruli. During acute pancreatitis, urinary AMY begins to increase about 12-24 hours after onset, and decreases more slowly than serum AMY. Therefore, it is more valuable to measure urinary AMY in the later stages of acute pancreatitis. In addition, in renal dysfunction, serum AMY is reduced.
Currently, the principle of the rate method is generally used for detecting amylase by using a fully automatic analyzer, for example, patent document No. CN108645846A discloses a method for measuring the activity of α -amylase of serum based on paper base, and adopts a two-point rate method.
Therefore, there is a need in the art to develop a method for detecting AMY to remove the effect of bilirubin on the detection.
Disclosure of Invention
Based on the above defects in the prior art, the invention provides a method for eliminating the influence of bilirubin on the absorbance detection of a serum sample, and improves the AMY detection method, so that a hemolyzed sample can also obtain a relatively accurate AMY value.
In order to achieve the purpose, the invention adopts the following technical scheme:
a detection method of α -amylase comprises the following steps:
s1, centrifuging the hemolysis sample to be detected, and sucking out serum after centrifugation;
s2, centrifuging the serum at a high speed, and sucking out the supernatant after centrifugation;
s3, mixing the supernatant and soluble starch in a buffer solution to obtain a solution to be detected;
s4, mixing the solution to be detected with sodium iodate and sodium bisulfite for reaction, detecting the absorbance at the wavelength of 630nm, and calculating the concentration of α -amylase in the hemolysis sample to be detected according to the absorbance.
Preferably, in step S1, the centrifugation process includes: the rotating speed is 1600-2000 rpm, and the time is 10-20 min.
Preferably, in step S2, the centrifugation process includes: the rotation speed is 16000-20000 rpm, and the time is 5-10 min.
Preferably, the buffer solution in step S3 is a phosphate buffer solution with ph 6.8.
Preferably, the phosphate buffer is a disodium hydrogen phosphate-sodium dihydrogen phosphate buffer or a disodium hydrogen phosphate-sodium dihydrogen phosphate buffer containing pancreatin.
Preferably, the concentration of the phosphate buffer solution is 50-100 mmol/L.
Preferably, the molar ratio of the sodium iodate to the sodium bisulfite is 1: (2.5-3).
Preferably, the concentration of the sodium iodate is 4-6 mmol/L.
Preferably, the soluble starch is dry powder, and is dissolved to the concentration of 600-800 mg/L before being mixed with the supernatant.
Preferably, in step S4, sodium iodate and sodium bisulfite are first mixed.
Compared with the prior art, the invention has the beneficial effects that:
(1) the method performs pretreatment on the hemolytic sample to be detected, namely performs centrifugal treatment on the hemolytic sample to be detected, and takes the supernatant for subsequent detection, so that the interference of the heme on the detection result can be reduced.
(2) According to the invention, sodium iodate and sodium bisulfite are used as color development liquid, the sodium iodate and the sodium bisulfite react in two steps to generate iodine, and the iodine is combined with unreacted starch to form a blue compound, so that the phenomenon that the color development of the reaction is influenced by the reduction of components caused by the fact that the iodine solution is easy to sublimate and volatilize when directly used is avoided, and the accuracy of a detection result is improved; compared with the prior art in which potassium iodide and acidic potassium iodide are used as color development liquids, the method has higher detection accuracy.
Detailed Description
The technical solution of the present invention will be further explained by the following specific examples.
Example 1:
α -amylase AMY is detected by adopting a full-automatic biochemical analyzer, and the sample is a blood sample.
The α -amylase detection method of the embodiment comprises the following steps:
(1) separating serum from a blood sample, then violently shaking the serum to cause artificial hemolysis, and obtaining a hemolyzed sample to be detected;
(2) centrifuging the hemolytic sample to be detected at 1600rpm for 10 minutes, and completely sucking out the upper serum;
(3) continuously centrifuging the serum sucked in the step (2) at 16000rpm for 10min, and sucking 50mL of supernatant;
(4) the reaction temperature of the semi-automatic biochemical analyzer is set to be 37 ℃, the reaction method is an end point method, the dominant wavelength is measured to be 630nm, and the reaction direction is a negative reaction. Mixing a hemolytic sample to be detected with 800mg/L soluble starch in a phosphate buffer solution with the pH value of 6.8, incubating for 360s, adding a mixed solution of 10mmol/L sodium bisulfite and 6mmol/L sodium iodate, uniformly mixing, placing in a semi-automatic biochemical analyzer, and detecting and recording the absorbance at the wavelength of 630 nm. Wherein the phosphate buffer solution is disodium hydrogen phosphate-sodium dihydrogen phosphate buffer solution or disodium hydrogen phosphate-sodium dihydrogen phosphate buffer solution containing pancreatin, and the concentration is 100 mmol/L; the molar ratio of sodium iodate to sodium bisulfite was 1: 2.5.
otherwise, the blank tube was treated as described above.
According to the calculation formula CSample (A)＝(ABlank space-ASample (A))/ABlank space×(C×V)/(t×VSample (A)) The α -amylase concentration in the test sample was calculated.
Wherein, CSample (A)The concentration of the hemolysis sample to be detected;
Asample (A)Is the absorbance of the hemolysis sample to be detected;
Ablank spaceAbsorbance of blank tube;
c is the concentration of soluble starch;
v is the volume of soluble starch;
t is reaction time (min);
Vsample (A)Is the volume of the hemolyzed sample to be tested。
Since the International units stipulate that hydrolysis of 4mg starch at 1min per liter of sample is 1 International Unit (U/L), it is necessary to convert the resulting amylase concentration to International units according to equation CSample (A)(International Unit) ═ CSample (A)X (1 × 1000)/4, wherein 1 is a reaction time (min) specified in international units; 1000 is the factor by which mL converts to L; 4 is the amount of hydrolyzed starch per liter of sample specified in international units.
Firstly, the accuracy analysis of the detection method of the embodiment:
nine clinical samples were taken, each according to the method and Gal-G described in this example2The CNP substrate method and the conventional method (the detection method disclosed in the patent publication No. CN 102288559B) for detecting the amylase content in a sample by using a CB171 semiautomatic biochemical analyzer. The concrete structure is as follows: and Gal-G2Compared with the CNP substrate method, the detection method of the embodiment has similar detection results, the correlation coefficient is 0.998, and the correlation coefficient is greater than that of the existing method, which indicates that the detection method of the embodiment has accurate and reliable detection results.
Second, the repeatability detection of the detection method of the embodiment
The coefficient of variation CV of α -amylase detected by the detection method of the embodiment is 1.65 percent and is less than Gal-G2The CNP substrate method and the existing method show that the detection method of the embodiment has better repeatability.
Example 2:
in this example, on the basis of example 1, the samples obtained in each step were tested:
specifically, a full-automatic biochemical analyzer is adopted to detect AMY, and the sample is a blood sample. Separating serum from a blood sample, sucking 50 mu L of the blood sample, and naming the sample as D1 to be detected, wherein the specific detection steps refer to example 1;
then, the residual serum is violently shaken to cause artificial hemolysis, a sample with hemolysis is firstly centrifuged at 1600rpm for 10min, the serum of the supernatant is completely sucked out, 50 mu L of the sample is taken, the sample is named D2 to be detected, and the specific detection steps refer to example 1;
the remaining serum was centrifuged for a further 10min at 16000rpm, the supernatant was aspirated for 50. mu.L and the sample was designated D3 for testing, the specific testing procedure referring to example 1.
The CV of D3 is 1.65%, and the CV of D1 and D2 are both more than 5% when D1, S2 and S3 are detected on a full-automatic biochemical analyzer.
In the above embodiment and its alternatives, the centrifugation rotation speed in step (2) may also be 1700rpm, 1800rpm, 1900rpm, 2000rpm, etc., and the centrifugation time may also be 12min, 15min, 16min, 18min, 20min, etc.
In the above embodiments and alternatives thereof, the centrifugation rotation speed in step (3) may also be 17000rpm, 18000rpm, 19000rpm, 20000rpm, etc., and the centrifugation time may also be 5min, 6min, 7min, 8min, 9min, etc.
In the above examples and alternatives, the concentration of the phosphate buffer may also be 50mmol/L, 60mmol/L, 80mmol/L, 90mmol/L, etc.
In the above examples and alternatives, the molar ratio of sodium iodate to sodium bisulfite may also be 1: 2.6, 1: 2.7, 1: 2.8, 1: 2.9, 1: 3, etc.
In the above examples and alternatives, the concentration of sodium iodate can also be 4mmol/L, 4.5mmol/L, 5mmol/L, 5.5mmol/L, and the like.
In the above examples and alternatives, the soluble starch is a dry powder that is solubilized to a concentration of 600mg/L, 650mg/L, 700mg/L, 750mg/L, etc., prior to mixing with the supernatant.
Claims (10)
1. An α -amylase detection method, which is characterized by comprising the following steps:
s1, centrifuging the hemolysis sample to be detected, and sucking out serum after centrifugation;
s2, centrifuging the serum at a high speed, and sucking out the supernatant after centrifugation;
s3, mixing the supernatant and soluble starch in a buffer solution to obtain a solution to be detected;
s4, mixing the solution to be detected with sodium iodate and sodium bisulfite for reaction, detecting the absorbance at the wavelength of 630nm, and calculating the concentration of α -amylase in the hemolysis sample to be detected according to the absorbance.
2. The method for detecting α -amylase as claimed in claim 1, wherein in the step S1, the centrifugation process comprises rotating at 1600-2000 rpm for 10-20 min.
3. The method for detecting α -amylase of claim 1, wherein in the step S2, the centrifugation process comprises rotating at 16000-20000 rpm for 5-10 min.
4. The method for detecting α -amylase according to claim 1, wherein the buffer solution in the step S3 is a phosphate buffer solution with pH 6.8.
5. The method of claim 4, wherein the phosphate buffer is a disodium hydrogen phosphate-sodium dihydrogen phosphate buffer or a disodium hydrogen phosphate-sodium dihydrogen phosphate buffer containing pancreatin.
6. The method for detecting α -amylase of claim 4, wherein the concentration of the phosphate buffer solution is 50-100 mmol/L.
7. The method for detecting α -amylase as claimed in claim 1, wherein the molar ratio of sodium iodate to sodium bisulfite is 1 (2.5-3).
8. The method for detecting α -amylase according to claim 1, wherein the concentration of sodium iodate is 4-6 mmol/L.
9. The method for detecting α -amylase of claim 1, wherein the soluble starch is dry powder, and is dissolved to a concentration of 600-800 mg/L before being mixed with the supernatant.
10. The method for detecting α -amylase according to claim 1, wherein in step S4, sodium iodate and sodium bisulfite are mixed.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201911392244.8A CN111157465A (en) | 2019-12-30 | 2019-12-30 | α -amylase detection method |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201911392244.8A CN111157465A (en) | 2019-12-30 | 2019-12-30 | α -amylase detection method |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN111157465A true CN111157465A (en) | 2020-05-15 |
Family
ID=70558913
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201911392244.8A Pending CN111157465A (en) | 2019-12-30 | 2019-12-30 | α -amylase detection method |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN111157465A (en) |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20030027347A1 (en) * | 2001-05-25 | 2003-02-06 | Phyllis Shapiro | Automated method for correcting blood analysis parameter results affected by interference from exogenous blood substitutes in whole blood, plasma, and serum |
| CN201188072Y (en) * | 2008-05-04 | 2009-01-28 | 黄友敏 | Apparatus for eliminating hemolysis |
| CN102288559A (en) * | 2011-06-09 | 2011-12-21 | 董理 | Method and kit for detecting amylase |
| CN106546729A (en) * | 2016-10-18 | 2017-03-29 | 上海凯璟生物科技有限公司 | A kind of new process for removing serum matrix effect in the detection of dry type immunofluorescence sizing technique |
-
2019
- 2019-12-30 CN CN201911392244.8A patent/CN111157465A/en active Pending
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20030027347A1 (en) * | 2001-05-25 | 2003-02-06 | Phyllis Shapiro | Automated method for correcting blood analysis parameter results affected by interference from exogenous blood substitutes in whole blood, plasma, and serum |
| CN201188072Y (en) * | 2008-05-04 | 2009-01-28 | 黄友敏 | Apparatus for eliminating hemolysis |
| CN102288559A (en) * | 2011-06-09 | 2011-12-21 | 董理 | Method and kit for detecting amylase |
| CN106546729A (en) * | 2016-10-18 | 2017-03-29 | 上海凯璟生物科技有限公司 | A kind of new process for removing serum matrix effect in the detection of dry type immunofluorescence sizing technique |
Non-Patent Citations (4)
| Title |
|---|
| 崔树宝等: "关于亚硫酸氢纳还原碘酸钾遇淀粉变蓝实验原理的讨论", 《天津化工》 * |
| 张丽霞等: "碘-淀粉吸光系数标准化法检测", 《中国医科大学学报》 * |
| 李玉芹: "血清肌钙蛋白-I均相化学发光免疫检测体系的初步建立", 《硕士电子期刊》 * |
| 高国生;姜俊;翁彭剑;: "不同标本因素对荧光定量PCR法测定HBV DNA结果的影响" * |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Giegel et al. | Manual and semi-automated procedures for measurement of triglycerides in serum | |
| CN102033050B (en) | Method for measuring pectin content in plant sample | |
| Maguire et al. | A continuous monitoring spectrophotometric method for the measurement of angiotensin-converting enzyme in human serum | |
| WO2010085413A1 (en) | Device and method for detection of humidity-compromised urine test strips | |
| CA2032053C (en) | Method for quantitation of calcium and magnesium | |
| CN1811391A (en) | Quantitative detecting method for the polyphenol content | |
| Aoyagi et al. | Rapid spectrophotometric determination of total phosphorus in industrial wastewaters by flow injection analysis including a capillary digestor | |
| Agatonović-Kuštrin et al. | Spectrophotometric study of diclofenac-Fe (III) complex | |
| CN106771147A (en) | A kind of quick diagnosis platelet-activating factor acetylhydro-lase kit and its application method | |
| Paroni et al. | Determination of creatinine in serum and urine by a rapid liquid-chromatographic method | |
| CN111157465A (en) | α -amylase detection method | |
| Anderson et al. | Urinary free catecholamines determined by liquid chromatography--fluorometry. | |
| Petrarulo et al. | Assay of plasma oxalate with soluble oxalate oxidase | |
| CN102033051B (en) | Continuous flow measuring method for pectin content in plant | |
| Hood | A–Z of clinical chemistry: a guide for the trainee | |
| Johansen et al. | Automated method for the determination of angiotensin-converting enzyme in serum | |
| Atkins et al. | Plasma concentrations of histamine measured by radioenzymatic assay: effects of histaminase incubations | |
| Hummerich et al. | Improvement of renin determination in human plasma using a commonly available renin standard in a radioimmunological method | |
| Holmes et al. | Automation of plasma antithrombin III assays. | |
| BE1009960A3 (en) | Reagent and method for determining metric ph-value in acid oils. | |
| WO2018056762A1 (en) | Reagent composition for measuring glycated albumin and method for measuring glycated albumin using same | |
| CN115420716B (en) | Method for detecting content of white hanging block and application thereof | |
| Moio et al. | Differential pHmeter determination of residual sugars in wine | |
| Boitieux et al. | Dissociation of immunocomplexes by ionic shock for the development of immunosensors: application to measurement of alpha 1-fetoprotein. | |
| CN114739933A (en) | Urea detection method based on enzymolysis 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 | ||
| RJ01 | Rejection of invention patent application after publication |
Application publication date: 20200515 |
|
| RJ01 | Rejection of invention patent application after publication |