DE2705859C2 - - Google Patents
Info
- Publication number
- DE2705859C2 DE2705859C2 DE2705859A DE2705859A DE2705859C2 DE 2705859 C2 DE2705859 C2 DE 2705859C2 DE 2705859 A DE2705859 A DE 2705859A DE 2705859 A DE2705859 A DE 2705859A DE 2705859 C2 DE2705859 C2 DE 2705859C2
- Authority
- DE
- Germany
- Prior art keywords
- glucose
- phosphate
- amylase
- reaction
- coenzyme
- 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.)
- Expired
Links
- 102000004139 alpha-Amylases Human genes 0.000 claims description 52
- 108090000637 alpha-Amylases Proteins 0.000 claims description 52
- 229940024171 alpha-amylase Drugs 0.000 claims description 52
- 238000006243 chemical reaction Methods 0.000 claims description 31
- 239000003153 chemical reaction reagent Substances 0.000 claims description 28
- 238000000034 method Methods 0.000 claims description 28
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 claims description 16
- 239000008103 glucose Substances 0.000 claims description 16
- 239000005515 coenzyme Substances 0.000 claims description 12
- BAWFJGJZGIEFAR-NNYOXOHSSA-N NAD zwitterion Chemical compound NC(=O)C1=CC=C[N+]([C@H]2[C@@H]([C@H](O)[C@@H](COP([O-])(=O)OP(O)(=O)OC[C@@H]3[C@H]([C@@H](O)[C@@H](O3)N3C4=NC=NC(N)=C4N=C3)O)O2)O)=C1 BAWFJGJZGIEFAR-NNYOXOHSSA-N 0.000 claims description 11
- 150000004676 glycans Chemical class 0.000 claims description 11
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 claims description 11
- 229920001282 polysaccharide Polymers 0.000 claims description 11
- 239000005017 polysaccharide Substances 0.000 claims description 11
- 108010057899 Maltose phosphorylase Proteins 0.000 claims description 10
- 102100031126 6-phosphogluconolactonase Human genes 0.000 claims description 9
- 108010029731 6-phosphogluconolactonase Proteins 0.000 claims description 9
- 108010018962 Glucosephosphate Dehydrogenase Proteins 0.000 claims description 9
- GUBGYTABKSRVRQ-ASMJPISFSA-N alpha-maltose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-ASMJPISFSA-N 0.000 claims description 9
- 239000007864 aqueous solution Substances 0.000 claims description 9
- 229930010764 α-maltose Natural products 0.000 claims description 9
- 239000004382 Amylase Substances 0.000 claims description 8
- 102000013142 Amylases Human genes 0.000 claims description 8
- 108010065511 Amylases Proteins 0.000 claims description 8
- VFRROHXSMXFLSN-UHFFFAOYSA-N Glc6P Natural products OP(=O)(O)OCC(O)C(O)C(O)C(O)C=O VFRROHXSMXFLSN-UHFFFAOYSA-N 0.000 claims description 8
- 235000019418 amylase Nutrition 0.000 claims description 8
- NBSCHQHZLSJFNQ-GASJEMHNSA-N D-Glucose 6-phosphate Chemical compound OC1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H](O)[C@H]1O NBSCHQHZLSJFNQ-GASJEMHNSA-N 0.000 claims description 7
- HXXFSFRBOHSIMQ-DVKNGEFBSA-N beta-D-glucose 1-phosphate Chemical compound OC[C@H]1O[C@@H](OP(O)(O)=O)[C@H](O)[C@@H](O)[C@@H]1O HXXFSFRBOHSIMQ-DVKNGEFBSA-N 0.000 claims description 7
- 230000015572 biosynthetic process Effects 0.000 claims description 7
- 238000006911 enzymatic reaction Methods 0.000 claims description 6
- 125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 claims description 6
- BIRSGZKFKXLSJQ-SQOUGZDYSA-N 6-Phospho-D-gluconate Chemical compound OP(=O)(O)OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(O)=O BIRSGZKFKXLSJQ-SQOUGZDYSA-N 0.000 claims description 5
- 108020001657 6-phosphogluconate dehydrogenase Proteins 0.000 claims description 5
- 102000004567 6-phosphogluconate dehydrogenase Human genes 0.000 claims description 5
- RWHOZGRAXYWRNX-VFUOTHLCSA-N alpha-D-glucose 1,6-bisphosphate Chemical compound O[C@H]1[C@H](O)[C@@H](COP(O)(O)=O)O[C@H](OP(O)(O)=O)[C@@H]1O RWHOZGRAXYWRNX-VFUOTHLCSA-N 0.000 claims description 4
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 claims description 4
- 150000002500 ions Chemical class 0.000 claims description 4
- 239000007857 degradation product Substances 0.000 claims description 3
- FNZLKVNUWIIPSJ-UHNVWZDZSA-N D-ribulose 5-phosphate Chemical compound OCC(=O)[C@H](O)[C@H](O)COP(O)(O)=O FNZLKVNUWIIPSJ-UHNVWZDZSA-N 0.000 claims description 2
- FNZLKVNUWIIPSJ-UHFFFAOYSA-N Rbl5P Natural products OCC(=O)C(O)C(O)COP(O)(O)=O FNZLKVNUWIIPSJ-UHFFFAOYSA-N 0.000 claims description 2
- XJLXINKUBYWONI-NNYOXOHSSA-N NADP zwitterion Chemical compound NC(=O)C1=CC=C[N+]([C@H]2[C@@H]([C@H](O)[C@@H](COP([O-])(=O)OP(O)(=O)OC[C@@H]3[C@H]([C@@H](OP(O)(O)=O)[C@@H](O3)N3C4=NC=NC(N)=C4N=C3)O)O2)O)=C1 XJLXINKUBYWONI-NNYOXOHSSA-N 0.000 claims 2
- 229920002472 Starch Polymers 0.000 description 19
- 235000019698 starch Nutrition 0.000 description 19
- 239000008107 starch Substances 0.000 description 17
- 102000004190 Enzymes Human genes 0.000 description 12
- 108090000790 Enzymes Proteins 0.000 description 12
- 238000004458 analytical method Methods 0.000 description 12
- 229940088598 enzyme Drugs 0.000 description 12
- 108091000115 phosphomannomutase Proteins 0.000 description 9
- 239000000243 solution Substances 0.000 description 8
- 239000000203 mixture Substances 0.000 description 6
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 6
- BOPGDPNILDQYTO-NNYOXOHSSA-N nicotinamide-adenine dinucleotide Chemical compound C1=CCC(C(=O)N)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 BOPGDPNILDQYTO-NNYOXOHSSA-N 0.000 description 6
- 239000007787 solid Substances 0.000 description 6
- 229920000856 Amylose Polymers 0.000 description 5
- 229920001503 Glucan Polymers 0.000 description 5
- 229950006238 nadide Drugs 0.000 description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 4
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 238000010521 absorption reaction Methods 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 230000007062 hydrolysis Effects 0.000 description 4
- 238000006460 hydrolysis reaction Methods 0.000 description 4
- LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 4
- 229920000945 Amylopectin Polymers 0.000 description 3
- XJLXINKUBYWONI-NNYOXOHSSA-O NADP(+) Chemical compound NC(=O)C1=CC=C[N+]([C@H]2[C@@H]([C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]3[C@H]([C@@H](OP(O)(O)=O)[C@@H](O3)N3C4=NC=NC(N)=C4N=C3)O)O2)O)=C1 XJLXINKUBYWONI-NNYOXOHSSA-O 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
- 150000001768 cations Chemical class 0.000 description 3
- 229910052816 inorganic phosphate Inorganic materials 0.000 description 3
- 229910052740 iodine Inorganic materials 0.000 description 3
- 239000011630 iodine Substances 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 244000005700 microbiome Species 0.000 description 3
- 210000002966 serum Anatomy 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 210000002700 urine Anatomy 0.000 description 3
- 108090001003 Beta-phosphoglucomutases Proteins 0.000 description 2
- 240000001929 Lactobacillus brevis Species 0.000 description 2
- 235000013957 Lactobacillus brevis Nutrition 0.000 description 2
- 241000192130 Leuconostoc mesenteroides Species 0.000 description 2
- 201000009906 Meningitis Diseases 0.000 description 2
- 241000588653 Neisseria Species 0.000 description 2
- 241001464937 Neisseria perflava Species 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 239000007795 chemical reaction product Substances 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- 102000010705 glucose-6-phosphate dehydrogenase activity proteins Human genes 0.000 description 2
- 108040005050 glucose-6-phosphate dehydrogenase activity proteins Proteins 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- 229910000160 potassium phosphate Inorganic materials 0.000 description 2
- 235000011009 potassium phosphates Nutrition 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- LEVVMZZBTOYKSC-UHFFFAOYSA-N 1-amino-4-hydroxybutane-2-sulfonic acid Chemical compound NCC(S(O)(=O)=O)CCO LEVVMZZBTOYKSC-UHFFFAOYSA-N 0.000 description 1
- QZTKDVCDBIDYMD-UHFFFAOYSA-N 2,2'-[(2-amino-2-oxoethyl)imino]diacetic acid Chemical compound NC(=O)CN(CC(O)=O)CC(O)=O QZTKDVCDBIDYMD-UHFFFAOYSA-N 0.000 description 1
- IHPYMWDTONKSCO-UHFFFAOYSA-N 2,2'-piperazine-1,4-diylbisethanesulfonic acid Chemical compound OS(=O)(=O)CCN1CCN(CCS(O)(=O)=O)CC1 IHPYMWDTONKSCO-UHFFFAOYSA-N 0.000 description 1
- ZCYVEMRRCGMTRW-UHFFFAOYSA-N 7553-56-2 Chemical compound [I] ZCYVEMRRCGMTRW-UHFFFAOYSA-N 0.000 description 1
- 229920001353 Dextrin Polymers 0.000 description 1
- 239000004375 Dextrin Substances 0.000 description 1
- 241000195619 Euglena gracilis Species 0.000 description 1
- 229920002527 Glycogen Polymers 0.000 description 1
- 241000186660 Lactobacillus Species 0.000 description 1
- 208000005647 Mumps Diseases 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 206010061902 Pancreatic neoplasm Diseases 0.000 description 1
- 206010033645 Pancreatitis Diseases 0.000 description 1
- 102000009569 Phosphoglucomutase Human genes 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 description 1
- FTNIPWXXIGNQQF-UHFFFAOYSA-N UNPD130147 Natural products OC1C(O)C(O)C(CO)OC1OC1C(CO)OC(OC2C(OC(OC3C(OC(OC4C(OC(O)C(O)C4O)CO)C(O)C3O)CO)C(O)C2O)CO)C(O)C1O FTNIPWXXIGNQQF-UHFFFAOYSA-N 0.000 description 1
- LUEWUZLMQUOBSB-UHFFFAOYSA-N UNPD55895 Natural products OC1C(O)C(O)C(CO)OC1OC1C(CO)OC(OC2C(OC(OC3C(OC(O)C(O)C3O)CO)C(O)C2O)CO)C(O)C1O LUEWUZLMQUOBSB-UHFFFAOYSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QUYVBRFLSA-N beta-maltose Chemical compound OC[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@@H]1O GUBGYTABKSRVRQ-QUYVBRFLSA-N 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 239000008366 buffered solution Substances 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 239000008367 deionised water Substances 0.000 description 1
- 229910021641 deionized water Inorganic materials 0.000 description 1
- 235000019425 dextrin Nutrition 0.000 description 1
- 239000001177 diphosphate Substances 0.000 description 1
- ZPWVASYFFYYZEW-UHFFFAOYSA-L dipotassium hydrogen phosphate Chemical compound [K+].[K+].OP([O-])([O-])=O ZPWVASYFFYYZEW-UHFFFAOYSA-L 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 230000007071 enzymatic hydrolysis Effects 0.000 description 1
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 229940096919 glycogen Drugs 0.000 description 1
- 239000008187 granular material Substances 0.000 description 1
- 230000031700 light absorption Effects 0.000 description 1
- 208000019423 liver disease Diseases 0.000 description 1
- 208000015486 malignant pancreatic neoplasm Diseases 0.000 description 1
- FJCUPROCOFFUSR-UHFFFAOYSA-N malto-pentaose Natural products OC1C(O)C(OC(C(O)CO)C(O)C(O)C=O)OC(CO)C1OC1C(O)C(O)C(OC2C(C(O)C(OC3C(C(O)C(O)C(CO)O3)O)C(CO)O2)O)C(CO)O1 FJCUPROCOFFUSR-UHFFFAOYSA-N 0.000 description 1
- UYQJCPNSAVWAFU-UHFFFAOYSA-N malto-tetraose Natural products OC1C(O)C(OC(C(O)CO)C(O)C(O)C=O)OC(CO)C1OC1C(O)C(O)C(OC2C(C(O)C(O)C(CO)O2)O)C(CO)O1 UYQJCPNSAVWAFU-UHFFFAOYSA-N 0.000 description 1
- FJCUPROCOFFUSR-GMMZZHHDSA-N maltopentaose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O[C@H]([C@H](O)CO)[C@H](O)[C@@H](O)C=O)O[C@H](CO)[C@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O[C@@H]2[C@@H]([C@@H](O)[C@H](O[C@@H]3[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O)[C@@H](CO)O2)O)[C@@H](CO)O1 FJCUPROCOFFUSR-GMMZZHHDSA-N 0.000 description 1
- LUEWUZLMQUOBSB-OUBHKODOSA-N maltotetraose Chemical compound O[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@H](CO)O[C@@H](O[C@@H]2[C@@H](O[C@@H](O[C@@H]3[C@@H](O[C@@H](O)[C@H](O)[C@H]3O)CO)[C@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O LUEWUZLMQUOBSB-OUBHKODOSA-N 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 208000010805 mumps infectious disease Diseases 0.000 description 1
- UIWVQFSAXYWENY-UHFFFAOYSA-N n'-ethylacetohydrazide Chemical compound CCNNC(C)=O UIWVQFSAXYWENY-UHFFFAOYSA-N 0.000 description 1
- 229920001542 oligosaccharide Polymers 0.000 description 1
- 150000002482 oligosaccharides Chemical class 0.000 description 1
- 201000002528 pancreatic cancer Diseases 0.000 description 1
- 208000008443 pancreatic carcinoma Diseases 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 235000021317 phosphate Nutrition 0.000 description 1
- 229940085991 phosphate ion Drugs 0.000 description 1
- 150000004804 polysaccharides Polymers 0.000 description 1
- 229920001592 potato starch Polymers 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000004043 responsiveness Effects 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 229960003080 taurine Drugs 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 238000010792 warming Methods 0.000 description 1
- 230000004580 weight loss Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/34—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving hydrolase
- C12Q1/40—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving hydrolase involving amylase
-
- 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
- G01N2333/902—Oxidoreductases (1.)
- G01N2333/904—Oxidoreductases (1.) acting on CHOH groups as donors, e.g. glucose oxidase, lactate dehydrogenase (1.1)
-
- 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
- G01N2333/91—Transferases (2.)
- G01N2333/912—Transferases (2.) transferring phosphorus containing groups, e.g. kinases (2.7)
- G01N2333/91205—Phosphotransferases in general
- G01N2333/9121—Phosphotransferases in general with an alcohol group as acceptor (2.7.1), e.g. general tyrosine, serine or threonine kinases
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Biochemistry (AREA)
- Physics & Mathematics (AREA)
- Molecular Biology (AREA)
- Biotechnology (AREA)
- Biophysics (AREA)
- Analytical Chemistry (AREA)
- Immunology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US05/657,976 US4036697A (en) | 1976-02-13 | 1976-02-13 | Kinetic assay for alpha-amylase |
| US05/758,518 US4097336A (en) | 1976-02-13 | 1977-01-11 | Reagent system for beta-amylase assay |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| DE2705859A1 DE2705859A1 (de) | 1977-08-18 |
| DE2705859C2 true DE2705859C2 (US07923587-20110412-C00022.png) | 1988-09-08 |
Family
ID=27097531
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DE19772705859 Granted DE2705859A1 (de) | 1976-02-13 | 1977-02-11 | Verfahren und reagenzsysteme zur analyse, insbesondere zur kinetischen analyse, von alpha- und beta-amylase, anorganischem phosphat sowie saurer phosphatase |
Country Status (11)
Families Citing this family (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA1068586A (en) * | 1976-07-01 | 1979-12-25 | Abbott Laboratories | .alpha.-AMYLASE ASSAY UTILIZING MODIFIED STARCH AS THE SUBSTRATE |
| AT362526B (de) * | 1977-09-13 | 1981-05-25 | Boehringer Mannheim Gmbh | Verfahren und reagens zur bestimmung von alpha- -amylase |
| DE2748036C2 (de) * | 1977-10-26 | 1986-08-21 | Boehringer Mannheim Gmbh, 6800 Mannheim | Verfahren zur Gewinnung von Maltose-phosphorylase oder/und β-Phosphoglucose-mutase und Verwendung derselben |
| EP0048035B1 (en) * | 1978-06-06 | 1983-12-07 | Flow General, Inc. | Maltodextrin phosphorylase limit dextrin and method of producing it |
| CA1187388A (en) * | 1978-09-20 | 1985-05-21 | American Monitor Corporation | Stabilization of working reagent solutions containing nadh, nadph, and/or enzymes, and the use of such stabilized reagents in enzymes or substrate assays |
| JPS5768798A (en) | 1980-10-14 | 1982-04-27 | Toyo Jozo Co Ltd | Novel measurement of amylase activity |
| US4360413A (en) * | 1980-12-29 | 1982-11-23 | Beckman Instruments, Inc. | Creatine kinase isoenzyme electrophoretic technique and improved creatine kinase isoenzyme reagent for use therein |
| JPS6010026U (ja) * | 1983-06-30 | 1985-01-23 | 松下電工株式会社 | 吊金具への軒樋の取付構造 |
| JPS6058729U (ja) * | 1983-09-30 | 1985-04-24 | 松下電工株式会社 | 軒樋支持装置 |
| JPH0520821Y2 (US07923587-20110412-C00022.png) * | 1986-07-07 | 1993-05-28 | ||
| US4990445A (en) * | 1988-01-20 | 1991-02-05 | Beckman Instruments, Inc. | Stable reagent and kinetic assay for alpha-amylase |
| JPH0227428U (US07923587-20110412-C00022.png) * | 1989-03-23 | 1990-02-22 | ||
| US5645558A (en) * | 1995-04-20 | 1997-07-08 | Medical University Of South Carolina | Anatomically shaped vasoocclusive device and method of making the same |
Family Cites Families (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR1508496A (fr) * | 1966-01-20 | 1968-01-05 | Warner Lambert Pharmaceutical | Produit et procédé pour le dosage de l'amylase |
| GB1366342A (en) * | 1970-07-28 | 1974-09-11 | Hayashibara Co | Process for the preparation of amylose |
| US3759794A (en) * | 1971-11-01 | 1973-09-18 | S Sax | Method for determination of amylase activity |
| US3888739A (en) * | 1973-05-07 | 1975-06-10 | Bio Reagents & Diagnostics Inc | Reagents and methods for determining amylase concentrations |
| US3879263A (en) * | 1973-09-06 | 1975-04-22 | Du Pont | Method for the determination of amylase |
| US4000042A (en) * | 1973-09-06 | 1976-12-28 | E. I. Du Pont De Nemours And Company | Diagnostic reagent for the determination of amylase |
| DE2741192C2 (de) * | 1977-09-13 | 1982-07-01 | Boehringer Mannheim Gmbh, 6800 Mannheim | Verfahren zur Bestimmung von alpha- Amylase |
-
1977
- 1977-01-11 US US05/758,518 patent/US4097336A/en not_active Expired - Lifetime
- 1977-01-31 IT IT19812/77A patent/IT1077151B/it active
- 1977-02-09 GB GB5238/77A patent/GB1540320A/en not_active Expired
- 1977-02-10 NO NO77770446A patent/NO155844C/no unknown
- 1977-02-10 JP JP1314977A patent/JPS52119296A/ja active Granted
- 1977-02-11 FR FR7703939A patent/FR2394804A1/fr active Granted
- 1977-02-11 SE SE7701564A patent/SE442406B/xx not_active IP Right Cessation
- 1977-02-11 NL NLAANVRAGE7701455,A patent/NL173285C/xx not_active IP Right Cessation
- 1977-02-11 DK DK061077A patent/DK160844C/da not_active IP Right Cessation
- 1977-02-11 DE DE19772705859 patent/DE2705859A1/de active Granted
- 1977-02-11 CA CA271,565A patent/CA1076935A/en not_active Expired
Also Published As
| Publication number | Publication date |
|---|---|
| IT1077151B (it) | 1985-05-04 |
| GB1540320A (en) | 1979-02-07 |
| NL173285B (nl) | 1983-08-01 |
| NL173285C (nl) | 1984-01-02 |
| FR2394804A1 (fr) | 1979-01-12 |
| DK61077A (da) | 1977-08-14 |
| US4097336A (en) | 1978-06-27 |
| JPS5527800B2 (US07923587-20110412-C00022.png) | 1980-07-23 |
| DK160844B (da) | 1991-04-22 |
| NO770446L (no) | 1977-08-16 |
| FR2394804B1 (US07923587-20110412-C00022.png) | 1981-12-18 |
| DE2705859A1 (de) | 1977-08-18 |
| SE442406B (sv) | 1985-12-23 |
| NO155844C (no) | 1987-06-17 |
| SE7701564L (sv) | 1977-08-14 |
| NO155844B (no) | 1987-03-02 |
| DK160844C (da) | 1991-10-07 |
| NL7701455A (nl) | 1977-08-16 |
| JPS52119296A (en) | 1977-10-06 |
| CA1076935A (en) | 1980-05-06 |
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