JPS58198758A - ヒトエノラーゼの定量方法 - Google Patents
ヒトエノラーゼの定量方法Info
- Publication number
- JPS58198758A JPS58198758A JP8177682A JP8177682A JPS58198758A JP S58198758 A JPS58198758 A JP S58198758A JP 8177682 A JP8177682 A JP 8177682A JP 8177682 A JP8177682 A JP 8177682A JP S58198758 A JPS58198758 A JP S58198758A
- Authority
- JP
- Japan
- Prior art keywords
- enolase
- antibody
- enzyme
- solid phase
- labeled
- 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
- 102000012288 Phosphopyruvate Hydratase Human genes 0.000 title claims abstract description 74
- 108010022181 Phosphopyruvate Hydratase Proteins 0.000 title claims abstract description 74
- 238000000034 method Methods 0.000 title claims abstract description 47
- 206010028980 Neoplasm Diseases 0.000 title claims abstract description 15
- 201000011510 cancer Diseases 0.000 title claims abstract description 9
- 102000004190 Enzymes Human genes 0.000 claims abstract description 28
- 108090000790 Enzymes Proteins 0.000 claims abstract description 28
- 239000007790 solid phase Substances 0.000 claims abstract description 19
- 230000000694 effects Effects 0.000 claims abstract description 10
- 210000001519 tissue Anatomy 0.000 claims description 9
- 210000001124 body fluid Anatomy 0.000 claims description 8
- 239000010839 body fluid Substances 0.000 claims description 8
- 239000012071 phase Substances 0.000 claims description 8
- 239000012634 fragment Substances 0.000 claims description 7
- 102000004169 proteins and genes Human genes 0.000 claims description 5
- 108090000623 proteins and genes Proteins 0.000 claims description 5
- 210000004369 blood Anatomy 0.000 claims description 4
- 239000008280 blood Substances 0.000 claims description 4
- 210000001175 cerebrospinal fluid Anatomy 0.000 claims description 4
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- 239000007795 chemical reaction product Substances 0.000 claims description 3
- 238000004393 prognosis Methods 0.000 claims description 3
- 230000001225 therapeutic effect Effects 0.000 claims description 3
- 210000002700 urine Anatomy 0.000 claims description 3
- 230000002209 hydrophobic effect Effects 0.000 claims description 2
- 210000003296 saliva Anatomy 0.000 claims description 2
- 150000003839 salts Chemical class 0.000 claims description 2
- 206010003445 Ascites Diseases 0.000 claims 1
- 108091005804 Peptidases Proteins 0.000 claims 1
- 206010036790 Productive cough Diseases 0.000 claims 1
- 239000004365 Protease Substances 0.000 claims 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 1
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- 230000035945 sensitivity Effects 0.000 abstract description 9
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- 239000007788 liquid Substances 0.000 abstract description 3
- 238000013399 early diagnosis Methods 0.000 abstract description 2
- 210000004412 neuroendocrine cell Anatomy 0.000 abstract description 2
- 239000000376 reactant Substances 0.000 abstract 2
- 230000036039 immunity Effects 0.000 abstract 1
- 102100028652 Gamma-enolase Human genes 0.000 description 44
- 210000002966 serum Anatomy 0.000 description 27
- 238000005259 measurement Methods 0.000 description 19
- 229940088598 enzyme Drugs 0.000 description 17
- 206010061902 Pancreatic neoplasm Diseases 0.000 description 9
- 208000015486 malignant pancreatic neoplasm Diseases 0.000 description 9
- 201000002528 pancreatic cancer Diseases 0.000 description 9
- 208000008443 pancreatic carcinoma Diseases 0.000 description 9
- 239000000243 solution Substances 0.000 description 9
- 206010029260 Neuroblastoma Diseases 0.000 description 8
- 210000002569 neuron Anatomy 0.000 description 7
- 241000473945 Theria <moth genus> Species 0.000 description 6
- 238000003127 radioimmunoassay Methods 0.000 description 6
- 238000001959 radiotherapy Methods 0.000 description 6
- 208000000461 Esophageal Neoplasms Diseases 0.000 description 5
- 206010017708 Ganglioneuroblastoma Diseases 0.000 description 5
- 206010058467 Lung neoplasm malignant Diseases 0.000 description 5
- 206010030155 Oesophageal carcinoma Diseases 0.000 description 5
- 208000015634 Rectal Neoplasms Diseases 0.000 description 5
- 210000004556 brain Anatomy 0.000 description 5
- 210000004027 cell Anatomy 0.000 description 5
- 201000004101 esophageal cancer Diseases 0.000 description 5
- 201000005202 lung cancer Diseases 0.000 description 5
- 208000020816 lung neoplasm Diseases 0.000 description 5
- 239000008363 phosphate buffer Substances 0.000 description 5
- 206010038038 rectal cancer Diseases 0.000 description 5
- 201000001275 rectum cancer Diseases 0.000 description 5
- 208000024891 symptom Diseases 0.000 description 5
- 108010044467 Isoenzymes Proteins 0.000 description 4
- 241000700159 Rattus Species 0.000 description 4
- 238000010586 diagram Methods 0.000 description 4
- 241000283973 Oryctolagus cuniculus Species 0.000 description 3
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 3
- 238000011088 calibration curve Methods 0.000 description 3
- 208000002458 carcinoid tumor Diseases 0.000 description 3
- 230000003247 decreasing effect Effects 0.000 description 3
- 150000004676 glycans Chemical class 0.000 description 3
- 230000003053 immunization Effects 0.000 description 3
- 229920001282 polysaccharide Polymers 0.000 description 3
- 239000005017 polysaccharide Substances 0.000 description 3
- 238000004445 quantitative analysis Methods 0.000 description 3
- 235000002639 sodium chloride Nutrition 0.000 description 3
- 230000002992 thymic effect Effects 0.000 description 3
- 238000011282 treatment Methods 0.000 description 3
- 210000004881 tumor cell Anatomy 0.000 description 3
- 244000115658 Dahlia pinnata Species 0.000 description 2
- 235000012040 Dahlia pinnata Nutrition 0.000 description 2
- 108010010803 Gelatin Proteins 0.000 description 2
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 2
- -1 alkaline phonupatase Proteins 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 102000005936 beta-Galactosidase Human genes 0.000 description 2
- 108010005774 beta-Galactosidase Proteins 0.000 description 2
- 239000013060 biological fluid Substances 0.000 description 2
- 210000005013 brain tissue Anatomy 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 238000002512 chemotherapy Methods 0.000 description 2
- 230000009260 cross reactivity Effects 0.000 description 2
- 201000010099 disease Diseases 0.000 description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
- 229920000159 gelatin Polymers 0.000 description 2
- 239000008273 gelatin Substances 0.000 description 2
- 235000019322 gelatine Nutrition 0.000 description 2
- 235000011852 gelatine desserts Nutrition 0.000 description 2
- 238000003018 immunoassay Methods 0.000 description 2
- 229940027941 immunoglobulin g Drugs 0.000 description 2
- 230000003211 malignant effect Effects 0.000 description 2
- 210000000944 nerve tissue Anatomy 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 238000011002 quantification Methods 0.000 description 2
- 229920002379 silicone rubber Polymers 0.000 description 2
- 239000004945 silicone rubber Substances 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- JQWHASGSAFIOCM-UHFFFAOYSA-M sodium periodate Chemical compound [Na+].[O-]I(=O)(=O)=O JQWHASGSAFIOCM-UHFFFAOYSA-M 0.000 description 2
- 125000006850 spacer group Chemical group 0.000 description 2
- 230000002485 urinary effect Effects 0.000 description 2
- IVLXQGJVBGMLRR-UHFFFAOYSA-N 2-aminoacetic acid;hydron;chloride Chemical compound Cl.NCC(O)=O IVLXQGJVBGMLRR-UHFFFAOYSA-N 0.000 description 1
- GXIURPTVHJPJLF-UWTATZPHSA-N 2-phosphoglycerate Natural products OC[C@H](C(O)=O)OP(O)(O)=O GXIURPTVHJPJLF-UWTATZPHSA-N 0.000 description 1
- GXIURPTVHJPJLF-UHFFFAOYSA-N 2-phosphoglyceric acid Chemical group OCC(C(O)=O)OP(O)(O)=O GXIURPTVHJPJLF-UHFFFAOYSA-N 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- BRLQWZUYTZBJKN-UHFFFAOYSA-N Epichlorohydrin Chemical compound ClCC1CO1 BRLQWZUYTZBJKN-UHFFFAOYSA-N 0.000 description 1
- 108010015776 Glucose oxidase Proteins 0.000 description 1
- 239000004366 Glucose oxidase Substances 0.000 description 1
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 208000008839 Kidney Neoplasms Diseases 0.000 description 1
- 102000013460 Malate Dehydrogenase Human genes 0.000 description 1
- 108010026217 Malate Dehydrogenase Proteins 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 206010038389 Renal cancer Diseases 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 206010041067 Small cell lung cancer Diseases 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 210000004100 adrenal gland Anatomy 0.000 description 1
- 210000004198 anterior pituitary gland Anatomy 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 210000003050 axon Anatomy 0.000 description 1
- WQZGKKKJIJFFOK-FPRJBGLDSA-N beta-D-galactose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-FPRJBGLDSA-N 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 210000000481 breast Anatomy 0.000 description 1
- 150000001718 carbodiimides Chemical class 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 210000005056 cell body Anatomy 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000024245 cell differentiation Effects 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 239000003431 cross linking reagent Substances 0.000 description 1
- 239000012531 culture fluid Substances 0.000 description 1
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- UFULAYFCSOUIOV-UHFFFAOYSA-N cysteamine Chemical compound NCCS UFULAYFCSOUIOV-UHFFFAOYSA-N 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 230000004069 differentiation Effects 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 210000003890 endocrine cell Anatomy 0.000 description 1
- 230000006870 function Effects 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 229940116332 glucose oxidase Drugs 0.000 description 1
- 235000019420 glucose oxidase Nutrition 0.000 description 1
- 235000011187 glycerol Nutrition 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 230000000984 immunochemical effect Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 201000010982 kidney cancer Diseases 0.000 description 1
- 201000007270 liver cancer Diseases 0.000 description 1
- 208000014018 liver neoplasm Diseases 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 229960003151 mercaptamine Drugs 0.000 description 1
- HOVAGTYPODGVJG-UHFFFAOYSA-N methyl beta-galactoside Natural products COC1OC(CO)C(O)C(O)C1O HOVAGTYPODGVJG-UHFFFAOYSA-N 0.000 description 1
- 229940072417 peroxidase Drugs 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 125000000843 phenylene group Chemical group C1(=C(C=CC=C1)*)* 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 238000002731 protein assay Methods 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 208000000587 small cell lung carcinoma Diseases 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 210000000225 synapse Anatomy 0.000 description 1
- 229920003002 synthetic resin Polymers 0.000 description 1
- 239000000057 synthetic resin Substances 0.000 description 1
- 210000001685 thyroid gland Anatomy 0.000 description 1
Classifications
-
- 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
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/574—Immunoassay; Biospecific binding assay; Materials therefor for cancer
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/90—Enzymes; Proenzymes
- G01N2333/914—Hydrolases (3)
- G01N2333/978—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5)
- G01N2333/986—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5) acting on amide bonds in cyclic amides (3.5.2), e.g. beta-lactamase (penicillinase, 3.5.2.6), creatinine amidohydrolase (creatininase, EC 3.5.2.10), N-methylhydantoinase (3.5.2.6)
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Immunology (AREA)
- Engineering & Computer Science (AREA)
- Hematology (AREA)
- Chemical & Material Sciences (AREA)
- Urology & Nephrology (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Physics & Mathematics (AREA)
- Biotechnology (AREA)
- Oncology (AREA)
- Hospice & Palliative Care (AREA)
- Food Science & Technology (AREA)
- Medicinal Chemistry (AREA)
- Cell Biology (AREA)
- Analytical Chemistry (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP8177682A JPS58198758A (ja) | 1982-05-15 | 1982-05-15 | ヒトエノラーゼの定量方法 |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP8177682A JPS58198758A (ja) | 1982-05-15 | 1982-05-15 | ヒトエノラーゼの定量方法 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS58198758A true JPS58198758A (ja) | 1983-11-18 |
| JPH038515B2 JPH038515B2 (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) | 1991-02-06 |
Family
ID=13755876
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP8177682A Granted JPS58198758A (ja) | 1982-05-15 | 1982-05-15 | ヒトエノラーゼの定量方法 |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPS58198758A (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) |
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2010032899A3 (en) * | 2008-09-22 | 2010-07-15 | Korea Research Institute Of Bioscience And Biotechnology | Eno1-specific human antibody |
| JP2013140030A (ja) * | 2011-12-28 | 2013-07-18 | Shimadzu Corp | 腎がん血中マーカー |
| CN107614517A (zh) * | 2015-04-01 | 2018-01-19 | 台北医学大学 | 抗感染疾病的抗体 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5347518A (en) * | 1976-10-07 | 1978-04-28 | Mochida Pharm Co Ltd | Immunologically measuring method |
| JPS56118671A (en) * | 1980-02-22 | 1981-09-17 | Amano Pharmaceut Co Ltd | Measuring method of specific enzyme immunity of hybrid type protein |
-
1982
- 1982-05-15 JP JP8177682A patent/JPS58198758A/ja active Granted
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5347518A (en) * | 1976-10-07 | 1978-04-28 | Mochida Pharm Co Ltd | Immunologically measuring method |
| JPS56118671A (en) * | 1980-02-22 | 1981-09-17 | Amano Pharmaceut Co Ltd | Measuring method of specific enzyme immunity of hybrid type protein |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2010032899A3 (en) * | 2008-09-22 | 2010-07-15 | Korea Research Institute Of Bioscience And Biotechnology | Eno1-specific human antibody |
| JP2013140030A (ja) * | 2011-12-28 | 2013-07-18 | Shimadzu Corp | 腎がん血中マーカー |
| CN107614517A (zh) * | 2015-04-01 | 2018-01-19 | 台北医学大学 | 抗感染疾病的抗体 |
| CN107614517B (zh) * | 2015-04-01 | 2022-01-21 | 台北医学大学 | 抗感染疾病的抗体 |
Also Published As
| Publication number | Publication date |
|---|---|
| JPH038515B2 (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) | 1991-02-06 |
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