GB2071318A - Reagent and Method for the Determination of Human-Muscle Aldolase - Google Patents
Reagent and Method for the Determination of Human-Muscle Aldolase Download PDFInfo
- Publication number
- GB2071318A GB2071318A GB8107059A GB8107059A GB2071318A GB 2071318 A GB2071318 A GB 2071318A GB 8107059 A GB8107059 A GB 8107059A GB 8107059 A GB8107059 A GB 8107059A GB 2071318 A GB2071318 A GB 2071318A
- Authority
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- United Kingdom
- Prior art keywords
- aldolase
- muscle
- antibody
- human
- solid phase
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- Granted
Links
- 108010068561 Fructose-Bisphosphate Aldolase Proteins 0.000 title claims abstract description 42
- 102000001390 Fructose-Bisphosphate Aldolase Human genes 0.000 title claims abstract description 42
- 238000000034 method Methods 0.000 title claims abstract description 33
- 239000003153 chemical reaction reagent Substances 0.000 title abstract description 8
- 210000003205 muscle Anatomy 0.000 claims abstract description 25
- 239000007790 solid phase Substances 0.000 claims abstract description 16
- 101000755879 Homo sapiens Fructose-bisphosphate aldolase A Proteins 0.000 claims abstract description 11
- 238000000926 separation method Methods 0.000 claims abstract description 11
- 101710123627 Fructose-bisphosphate aldolase A Proteins 0.000 abstract description 6
- 102100022277 Fructose-bisphosphate aldolase A Human genes 0.000 abstract description 6
- 241000282414 Homo sapiens Species 0.000 description 13
- 238000006243 chemical reaction Methods 0.000 description 10
- 239000000427 antigen Substances 0.000 description 8
- 230000000694 effects Effects 0.000 description 8
- 239000000243 solution Substances 0.000 description 8
- 102000036639 antigens Human genes 0.000 description 7
- 108091007433 antigens Proteins 0.000 description 7
- 239000007853 buffer solution Substances 0.000 description 7
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 7
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- GNGACRATGGDKBX-UHFFFAOYSA-N dihydroxyacetone phosphate Chemical compound OCC(=O)COP(O)(O)=O GNGACRATGGDKBX-UHFFFAOYSA-N 0.000 description 4
- 239000002504 physiological saline solution Substances 0.000 description 4
- 238000003127 radioimmunoassay Methods 0.000 description 4
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 3
- 108010044467 Isoenzymes Proteins 0.000 description 3
- 241000124008 Mammalia Species 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- 229910019142 PO4 Inorganic materials 0.000 description 3
- 239000004793 Polystyrene Substances 0.000 description 3
- 239000012153 distilled water Substances 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 239000010452 phosphate Substances 0.000 description 3
- 229920002223 polystyrene Polymers 0.000 description 3
- NLKNQRATVPKPDG-UHFFFAOYSA-M potassium iodide Chemical compound [K+].[I-] NLKNQRATVPKPDG-UHFFFAOYSA-M 0.000 description 3
- 210000002966 serum Anatomy 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- 229920000936 Agarose Polymers 0.000 description 2
- 241000271566 Aves Species 0.000 description 2
- 229920002307 Dextran Polymers 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- RFSUNEUAIZKAJO-ARQDHWQXSA-N Fructose Chemical compound OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O RFSUNEUAIZKAJO-ARQDHWQXSA-N 0.000 description 2
- 229930091371 Fructose Natural products 0.000 description 2
- 239000005715 Fructose Substances 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 229920002684 Sepharose Polymers 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 201000011510 cancer Diseases 0.000 description 2
- VDQQXEISLMTGAB-UHFFFAOYSA-N chloramine T Chemical compound [Na+].CC1=CC=C(S(=O)(=O)[N-]Cl)C=C1 VDQQXEISLMTGAB-UHFFFAOYSA-N 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 239000012847 fine chemical Substances 0.000 description 2
- 238000002523 gelfiltration Methods 0.000 description 2
- 238000002372 labelling Methods 0.000 description 2
- 210000004185 liver Anatomy 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- 229910000029 sodium carbonate Inorganic materials 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 229960001479 tosylchloramide sodium Drugs 0.000 description 2
- MJQHZNBUODTQTK-UHFFFAOYSA-N 2-[[3-[2-[(3,4-dihydroxy-2,6-dioxabicyclo[3.2.1]octan-8-yl)oxy]-3,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-4-hydroxy-2,6-dioxabicyclo[3.2.1]octan-8-yl]oxy]-6-(hydroxymethyl)oxane-3,4,5-triol Chemical compound OC1C(O)C(O)C(CO)OC1OC1C2OCC1OC(OC1C(C(OC3C4OCC3OC(O)C4O)OC(CO)C1O)O)C2O MJQHZNBUODTQTK-UHFFFAOYSA-N 0.000 description 1
- 241000272525 Anas platyrhynchos Species 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 102000004317 Lyases Human genes 0.000 description 1
- 108090000856 Lyases Proteins 0.000 description 1
- 206010029719 Nonspecific reaction Diseases 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 108010058846 Ovalbumin Proteins 0.000 description 1
- 206010061902 Pancreatic neoplasm Diseases 0.000 description 1
- 241000009328 Perro Species 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 208000005718 Stomach Neoplasms Diseases 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 150000001299 aldehydes Chemical class 0.000 description 1
- 238000005882 aldol condensation reaction Methods 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 230000004069 differentiation Effects 0.000 description 1
- 230000003292 diminished effect Effects 0.000 description 1
- 239000001177 diphosphate Substances 0.000 description 1
- 230000037149 energy metabolism Effects 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 239000011888 foil Substances 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 230000034659 glycolysis Effects 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 201000011061 large intestine cancer Diseases 0.000 description 1
- 235000021184 main course Nutrition 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 230000029052 metamorphosis Effects 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 229920001296 polysiloxane Polymers 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 239000000376 reactant Substances 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- HRZFUMHJMZEROT-UHFFFAOYSA-L sodium disulfite Chemical compound [Na+].[Na+].[O-]S(=O)S([O-])(=O)=O HRZFUMHJMZEROT-UHFFFAOYSA-L 0.000 description 1
- 235000010262 sodium metabisulphite Nutrition 0.000 description 1
- 239000004296 sodium metabisulphite Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 239000012086 standard solution Substances 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/40—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against enzymes
-
- 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
- G01N33/573—Immunoassay; Biospecific binding assay; Materials therefor for enzymes or isoenzymes
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Immunology (AREA)
- Molecular Biology (AREA)
- Engineering & Computer Science (AREA)
- Urology & Nephrology (AREA)
- General Health & Medical Sciences (AREA)
- Hematology (AREA)
- Medicinal Chemistry (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- Organic Chemistry (AREA)
- Biotechnology (AREA)
- Physics & Mathematics (AREA)
- Cell Biology (AREA)
- Genetics & Genomics (AREA)
- Microbiology (AREA)
- Biophysics (AREA)
- Food Science & Technology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Analytical Chemistry (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
Abstract
A reagent for the determination of human-muscle type aldolase comprises radioisotope-labelled muscle aldolase antibody and a determination process comprises the following steps: (a) contacting a sample with insolubilized muscle aldolase antibody, followed by separation of the solid phase; (b) contacting the solid phase with radioisotope-labelled muscle type aldolase antibody, followed by separation of the solid phase; and (c) determining the radioactivity of the solid phase. l
Description
SPECIFICATION
Reagent and Method for the Determination of
Human-muscle Aldolase
This invention relates to reagents and methods for the determination of the human-muscle aldolase.
Aldolase is a general term for the enzymes which catalyze the aldol condensation between dihydroxyacetone phosphate and a variety of aldehydes, as well as catalyzing the reverse process. This invention is concerned with fructose diphosphate aldolase (E.C. 4. 1. 2. 13, fructose
1 ,6-phosphate-D-glycelaldehyde-3-phosphate lyase) which reversibly decomposes fructose-i ,6diphosphate into dihydroxyacetone phosphate and D-glyceladehyde-3-phosphate. This enzyme occupies the main course of the glycolysis system, and in particular is distributed mainly in muscle, thereby contributing importantly to energy metabolism.
Mammal aldolase comprises three types of isoenzymes, that is, the muscle type (A type), the liver type (B type) and the brain type (C type). It is known that the ratio of these isoenzymes varies in accordance with the metamorphosis of the living body, such as differentiation of the fetal liver in rat, canceration or organism in human, rat, and the like.
There have been conventionally known two methods for determining the human-muscle aldolase, one of which is the electrophoretic method, and the other is a method which comprises measuring the decomposition activities of two substrates for aldolase, that is, fructose 1 6-diphosphate (FDP) and fructose-l -phosphate (FIP) [FDP-ALD activity and FIP-ALD activity], thereby determining the activity ratio (FDP/FIP).
These methods, however, involve various problems.
In the electrophoretic method, the problem is that the migration points of the human aldolase isoenzymes are positioned so closely to one another that discrimination is difficult and precise quantitative determination can not be achieved.
In the method of measuring the activity ratio
FDP/FIP, operation is particularly complicated for the measurement of the FIP-ALD activity, accompanied by no quantitative determination.
Recently, there has been reported a method for determining aldolase by means of radioimmunoassay through competition (double antibody method). Compared with the aforementioned methods, this method has better sensitivity and quantification. However, this method also has some disadvantage in that there is required a large amount of the second antibody for the separation of B and F. Moreover, the handling procedure itself for the separation is very complicated, taking a long time and requiring much labour. There is further observed some nonspecific reaction.
The present invention provides a radioisotopelabelled muscle aldolase antibody. Such a product can be used in a method of the invention for the determination of the human-muscle aldolase by means of radioimmunoassay using the so-called "Sandwich method" with the aldolase antibody as a reagent.
By this method of the invention, various defects in the methods of prior art can be avoided or diminished. More particularly, the method of the present invention is remarkable in both the sensitivity for the determination and the quantitative effect. Also in comparison with the double-antibody method, the method of the present invention is characterized in that the second antibody is not required; the separation procedure for B and F is simple and convenient; and non-specific reaction is outstandingly low.
According to the Sandwich-method of the present invention, determination of humanmuscle type aldolase is carried out through the following steps:
(a) contacting a sample with an insolubilized muscle aldolase antibody, followed by separation of the solid phase;
(b) contacting the solid phase with a radioisotope-labelled muscle aldolase antibody, followed by separation of the solid phase; and
(c) determining the radioactivity of the solid phase.
The following will illustrate more particularly this method.
In the step (a), an antibodyinsolubilized by combination with a carrier is incubated together with a specimen, such as serum, etc, so that the antigen (human muscle aldolase) in the specimen may react with the insolubilized antibody. After the reaction is over, the reaction solution is removed and the solid phase is washed with buffer solution, distilled water, physiological saline water or the like.
In the step (b), the solid phase obtained in the step (a) is incubated together with a radioisotopelabelled antibody, resulting in that the radioisotope-labelled antibody combines with the antigen previously combined with the insolubilized antibody. After the reaction is over, the reaction solution is removed, and the solid phase is washed with a buffer solution, distilled water, physiological saline water or the like.
In the step (c), the radioactivity of the solid phase obtained in the step (b) is determined using a well-type scintillation counter or the like.
The radioactivity of standard samples of the antigen is previously measured with the determination system, so as to set up a standard curve for the amount of antigen versus the radioactivity. The radioactivity of a sample is measured with the same determination system, and then the amount of antigen in the specimen is determined from the standard curve.
The following description further illustrates the reagent for determination to be used with the present method and the muscle aldolase antibody to be used with the production of the reagent.
A) The Muscle Aldolase Antibody
Antiserum is obtained by using the muscle type aldolase of a mammal such as human, rabbit, dog, monkey, etc, to immunize another animal.
The immunized animal is preferably selected from species of birds, because the muscle type aldolases do not show significant immunological distinction between the mammals. Iltustrative of the preferred birds include, for example, fowl, turkey, duck and the like.
In the purification of the resulting antiserum, there can be used a method which comprises adding the inactivated serum of the animal which is the source of the muscle type aldolase, and removing by absorption the other impure antibody; or affinity chromatography using support combined the muscle type aldolase; or the like.
B) Radioisotope-labelled Muscle Aldolase
Antibody
The labelling of muscle type aldolase antibody by means of radioisotope can be achieved by any conventional methods.
For example, the labelling is carried out by the chloramine-T method using 1251, 13'1, etc, as the radioisotope, or by the like method.
C) The Insolubilized Muscle Aldolase Antibody
As a carrier, there is used an insoluble solid which is combinative with the antibody.
Illustrative of such solids include, for example,
polystyrene, cellulose, aga rose, glass, bridged
dextran, metal, etc. The solid can take any suitable form, such as tube, microtiter plate,
powder, sphere, disc, plate, foil, etc.
In the case of a polystyrene microtiter plate,
the antibody may combine with the wall surface of the plate; when the antibody is properly diluted with a buffer solution or the like, the diluted solution is then added to the plate, and the whole is finally allowed to stand.
The above description relates to the sandwich
method, but the human muscle aldolase can be
also determined by immunoradiometric assay
using radioisotope-labelled muscle aldolase
antibody which is the reagent of the present
invention. This method comprises reacting the
radioisotope-labelled antibody with a sample
(antigen), followed by separation of the
radioisotope-label led antibody-antigen reactant
(B) frorr. unreacted radioisotope-labelled antibody
(F), and determining the radioactivity of either (B) or (F). For the separation of (B) and (F), one can
use gel filtration, an absorption by means of
insolubilized antigen, etc.
The following experiments and examples will further illustrate this invention.
The figure of the attached drawing shows a
standard curve for the human-muscle aldolase obtained by the radioimmunoassay in the following Example 2.
Experiment 1
Human Muscle Aldolase Antibody.
The human-muscle aldolase (1 mg) was
dissolved in physiological salt water (0.5 ml), and
with the solution was admixed an equal volume of
Freund complete adjuvant. The product was
immunized by subcutaneous injection in a fowl
(White Leghorn) at 4 intervals of one week, so
that the injections amounted to five times. One
week after the last immunization, the blood was
collected from the fowl to obtain the anti-serum.
Sepharose 4B (Trade Mark of Pharmacia Fine
Chemicals AB; Agarose) (10 g) which was
activated with bromo-cyanide, and the human
muscle type aldolase (10 mg), were allowed to
stand at 40C overnight in 15 ml 0.1 M sodium
carbonate buffer solution (pH 9.0).
The resulting Sepharose 4B gel combined with the human-muscle type aldolase was packed into a column, and washed with 0.05 m trishydrochloric acid buffer solution (pH 8.0) containing 0.5 N sodium chloride. To this column was added the above-mentioned human-muscle aldolase anti-serum, and the anti-serum was eluted with 0.05 M tris-hydrochloric acid buffer solution (pH 8.0) containing 0.5 N sodium chloride. Thereafter, 0.1 M aqueous sodium carbonate solution was added to the column to elute the human-muscle aldolase antibody. The antibody eluate was subjected to dialysis with 0.05 M tris-hydrochloric acid buffer solution (pH 8.0) to obtain 3 mg of the human muscle aldolase antibody.
Experiment 2
Insolubilized Human-muscle Aldolase
Antibody
Into each of the holes provided on a polystyrene microtiter plate was added 200,ul of solution of the human-muscle aldolase antibody, adjusted to OD28o=0.10, and the plate then allowed to stand overnight at 40C. The solution was removed from the plate. The plate was washed with distilled water, giving the microtiter
plate with combined human-muscle type aldolase
antibody.
Example 1 '251-labelled Human Muscle Aldolase Antibody Na1251 of 250 iicude (10,t41),0.5 M phosphate buffer (pH 7.4 (12.5 'it), human muscle aldolase antibody (1.85 mg/ml) (10 yI) and Chloramine-T (3 mg/mi) (12.5 yI) were reacted with one another for 20 seconds in a small test tube coated with silicone. After the reaction was over, sodium metabisulphite (6 mg/ml) (25 M1) were added to the mixture, so as to stop the reaction. To the resulting mixture were added potassium iodide (50 mg/ml) (12.5 MI) and 2% egg albumin (250 ,ul) in 0.05 M phosphate buffer. The whole was then subjected to gel-filtration by means of
Sephadex G-25 M (Trade Mark Pharmacia Fine
Chemicals AB; bridged-dextran), so that the free '251 may be removed. There was thus obtained '251-labelled human muscle aldolase antibody, The specific activity thereof being 11.6 u curie/ug.
Example 2
Radioimmunoassay (Sandwich Method)
Into each of the holes which were provided on the microtiter plate combined with human muscle type aldolase antibody, 100 yl of the standard solution of the human muscle aldolase were respectively added. The whole was reacted at 370C for 2 hours. After the reaction was over, the supernatant layer was removed, and the remainder was washed thrice with physiological saline solution. To each of the washed holes was then added 100,us of '251-labelled human muscle type aldolase antibody (about 200,000 cpm).
Reaction was allowed to proceed at room temperature for 1 6 hours. After the reaction was over, the supernatant layer was removed. The remainder was washed thrice with physiological saline solution. After the contained water was thoroughly exhausted, the plate was cut, and the respective hole portions were separated from each other. The individual aliquots were respectively placed in small test tubes.
Radioactivity was counted in a well-type scintilation counter.
As shown in Figure 1, there was obtained a standard curve wherein about 8-1 000 ng/ml were plotted as measurable ranges. In the Figure, the horizontal axis (logarithm) indicates the concentration (ng/ml) of the human muscle aldolase, and the vertical axis indicates the radioactivity (cpm).
Human muscle type aldolases in various human serums were then determined through the above assay system. it was thus observed that the human muscle type aldolase of 25 normal subjects amounts to 165+40 ng/ml, all of which were less than 210 ng/ml. To the contrary, the human muscle type aldolase of 20 cancer patients showed higher values than 210 ng/ml, with two exceptions. The 20 cancer patients comprised 7 heptamae, 8 gastric cancers, 3 large intestine cancers, and 2 pancreatic cancers.
Claims (4)
1. Radioisotope-labelled muscle aldolase antibody.
2. Antibody according to claim 1, wherein the radioisotope is 1251.
3. Antibody according to claim 1, wherein the muscle aldolase antibody is human-muscle type aldolase antibody.
4. A process for the determination of humanmuscle aldolase which comprises the following steps:
(a) contacting a sample with an insolubilized muscle aldolase antibody, followed by separation of the, solid phase;
(b) contacting the solid phase with radioisotope-labelled muscle aldolase antibody, followed by separation of the solid phase; and
(c) determining the radioactivity of the solid phase.
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2799680A JPS56125667A (en) | 1980-03-07 | 1980-03-07 | Reagent for measurement and measuring method for human muscle type aldolase |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| GB2071318A true GB2071318A (en) | 1981-09-16 |
| GB2071318B GB2071318B (en) | 1983-08-24 |
Family
ID=12236425
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| GB8107059A Expired GB2071318B (en) | 1980-03-07 | 1981-03-06 | Reagent and method for the determination of human-muscle aldolase |
Country Status (10)
| Country | Link |
|---|---|
| JP (1) | JPS56125667A (en) |
| BE (1) | BE887828A (en) |
| CA (1) | CA1141291A (en) |
| CH (1) | CH651933A5 (en) |
| DE (1) | DE3107268A1 (en) |
| FR (1) | FR2477573A1 (en) |
| GB (1) | GB2071318B (en) |
| IT (1) | IT1136853B (en) |
| NL (1) | NL8101068A (en) |
| SE (1) | SE8101404L (en) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB2161166A (en) * | 1984-07-03 | 1986-01-08 | Du Pont | Radiolabeling of methionine containing proteins and peptides |
| WO2006067792A2 (en) * | 2004-12-22 | 2006-06-29 | Yeda Research And Development Co. Ltd. At The Weizmann Institute Of Science | Aldolase autoantigens useful in diagnosis and treatment of alzheimer's disease |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH0672893B2 (en) * | 1985-08-16 | 1994-09-14 | 富士薬品工業株式会社 | Determination of human prolyl hydroxylase in human blood by radioimmunoassay. |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5648894A (en) * | 1979-09-25 | 1981-05-02 | Eisai Co Ltd | Reagent for measuring human muscular aldolase and its determination |
-
1980
- 1980-03-07 JP JP2799680A patent/JPS56125667A/en active Pending
-
1981
- 1981-02-26 DE DE19813107268 patent/DE3107268A1/en not_active Withdrawn
- 1981-03-02 CH CH1389/81A patent/CH651933A5/en not_active IP Right Cessation
- 1981-03-03 FR FR8104174A patent/FR2477573A1/en active Pending
- 1981-03-04 IT IT20117/81A patent/IT1136853B/en active
- 1981-03-04 SE SE8101404A patent/SE8101404L/en unknown
- 1981-03-05 NL NL8101068A patent/NL8101068A/en not_active Application Discontinuation
- 1981-03-06 BE BE0/204036A patent/BE887828A/en not_active IP Right Cessation
- 1981-03-06 CA CA000372438A patent/CA1141291A/en not_active Expired
- 1981-03-06 GB GB8107059A patent/GB2071318B/en not_active Expired
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB2161166A (en) * | 1984-07-03 | 1986-01-08 | Du Pont | Radiolabeling of methionine containing proteins and peptides |
| WO2006067792A2 (en) * | 2004-12-22 | 2006-06-29 | Yeda Research And Development Co. Ltd. At The Weizmann Institute Of Science | Aldolase autoantigens useful in diagnosis and treatment of alzheimer's disease |
| WO2006067792A3 (en) * | 2004-12-22 | 2007-05-03 | Yeda Res & Dev | Aldolase autoantigens useful in diagnosis and treatment of alzheimer's disease |
Also Published As
| Publication number | Publication date |
|---|---|
| NL8101068A (en) | 1981-10-01 |
| GB2071318B (en) | 1983-08-24 |
| SE8101404L (en) | 1981-09-08 |
| FR2477573A1 (en) | 1981-09-11 |
| BE887828A (en) | 1981-07-01 |
| DE3107268A1 (en) | 1982-01-07 |
| IT1136853B (en) | 1986-09-03 |
| IT8120117A0 (en) | 1981-03-04 |
| JPS56125667A (en) | 1981-10-02 |
| CA1141291A (en) | 1983-02-15 |
| CH651933A5 (en) | 1985-10-15 |
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