CA1068586A - DOSAGE DE L'ACTIVITE DE L'.alpha.-AMYLASE SUR UN SUBSTRAT D'AMIDON MODIFIE - Google Patents

DOSAGE DE L'ACTIVITE DE L'.alpha.-AMYLASE SUR UN SUBSTRAT D'AMIDON MODIFIE

Info

Publication number: CA1068586A
Authority: CA; Canada
Prior art keywords: phosphate; amylase; glucose; alpha; sample
Prior art date: 1976-07-01
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

Application number

CA281,158A

Other languages

English (en)

Inventor

Charles Y. Huang

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Abbott Laboratories

Original Assignee

Abbott Laboratories

Priority date (The priority date 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 date listed.)

1976-07-01

Filing date

1977-06-22

Publication date

1979-12-25

1977-06-22 Application filed by Abbott Laboratories filed Critical Abbott Laboratories

1979-12-25 Application granted granted Critical

1979-12-25 Publication of CA1068586A publication Critical patent/CA1068586A/fr

Status Expired legal-status Critical Current

Links

239000004382 Amylase Substances 0.000 title claims abstract description 31
239000000758 substrate Substances 0.000 title claims abstract description 19
229920000881 Modified starch Polymers 0.000 title claims abstract description 8
239000004368 Modified starch Substances 0.000 title claims abstract description 8
235000019426 modified starch Nutrition 0.000 title claims abstract description 8
238000003556 assay Methods 0.000 title description 11
238000000034 method Methods 0.000 claims abstract description 32
102000004190 Enzymes Human genes 0.000 claims abstract description 12
108090000790 Enzymes Proteins 0.000 claims abstract description 12
229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 claims abstract description 11
238000005859 coupling reaction Methods 0.000 claims abstract description 9
210000002966 serum Anatomy 0.000 claims abstract description 9
102100031126 6-phosphogluconolactonase Human genes 0.000 claims abstract description 8
108010029731 6-phosphogluconolactonase Proteins 0.000 claims abstract description 8
108010018962 Glucosephosphate Dehydrogenase Proteins 0.000 claims abstract description 8
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 claims abstract 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 abstract description 7
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 abstract description 7
102000009569 Phosphoglucomutase Human genes 0.000 claims abstract description 7
230000008878 coupling Effects 0.000 claims abstract description 7
238000010168 coupling process Methods 0.000 claims abstract description 7
108091000115 phosphomannomutase Proteins 0.000 claims abstract description 7
230000009471 action Effects 0.000 claims abstract description 4
HXXFSFRBOHSIMQ-VFUOTHLCSA-N alpha-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-VFUOTHLCSA-N 0.000 claims abstract 2
229950010772 glucose-1-phosphate Drugs 0.000 claims abstract 2
239000003153 chemical reaction reagent Substances 0.000 claims description 17
108010073135 Phosphorylases Proteins 0.000 claims description 14
102000009097 Phosphorylases Human genes 0.000 claims description 14
UDMBCSSLTHHNCD-UHFFFAOYSA-N Coenzym Q(11) Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(O)=O)C(O)C1O UDMBCSSLTHHNCD-UHFFFAOYSA-N 0.000 claims description 6
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 6
UDMBCSSLTHHNCD-KQYNXXCUSA-N adenosine 5'-monophosphate Chemical group C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]1O UDMBCSSLTHHNCD-KQYNXXCUSA-N 0.000 claims description 6
229950006790 adenosine phosphate Drugs 0.000 claims description 6
150000004676 glycans Chemical class 0.000 claims description 6
229920001282 polysaccharide Polymers 0.000 claims description 6
239000005017 polysaccharide Substances 0.000 claims description 6
RXGJTUSBYWCRBK-UHFFFAOYSA-M 5-methylphenazinium methyl sulfate Chemical compound COS([O-])(=O)=O.C1=CC=C2[N+](C)=C(C=CC=C3)C3=NC2=C1 RXGJTUSBYWCRBK-UHFFFAOYSA-M 0.000 claims description 3
239000012992 electron transfer agent Substances 0.000 claims description 3
230000000813 microbial effect Effects 0.000 claims description 3
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 2
241000192132 Leuconostoc Species 0.000 claims description 2
240000004808 Saccharomyces cerevisiae Species 0.000 claims description 2
239000013060 biological fluid Substances 0.000 claims description 2
238000005259 measurement Methods 0.000 claims description 2
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 claims 2
JJMQRJKPLUACSO-UHFFFAOYSA-N 3-(4-iodophenyl)-2-(4-nitrophenyl)-5-phenyl-1,3-dihydrotetrazol-3-ium;chloride Chemical group [Cl-].C1=CC([N+](=O)[O-])=CC=C1N1N(C=2C=CC(I)=CC=2)[NH2+]C(C=2C=CC=CC=2)=N1 JJMQRJKPLUACSO-UHFFFAOYSA-N 0.000 claims 1
ACFIXJIJDZMPPO-NNYOXOHSSA-N NADPH 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](OP(O)(O)=O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 ACFIXJIJDZMPPO-NNYOXOHSSA-N 0.000 claims 1
229910019142 PO4 Inorganic materials 0.000 claims 1
239000012190 activator Substances 0.000 claims 1
239000007788 liquid Substances 0.000 claims 1
229940101270 nicotinamide adenine dinucleotide (nad) Drugs 0.000 claims 1
NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 claims 1
239000010452 phosphate Substances 0.000 claims 1
239000007787 solid Substances 0.000 claims 1
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims 1
229920002472 Starch Polymers 0.000 abstract description 16
235000019698 starch Nutrition 0.000 abstract description 16
239000008107 starch Substances 0.000 abstract description 15
238000006243 chemical reaction Methods 0.000 abstract description 10
230000015572 biosynthetic process Effects 0.000 abstract description 5
230000000694 effects Effects 0.000 abstract description 5
238000002835 absorbance Methods 0.000 abstract description 4
210000002700 urine Anatomy 0.000 abstract description 4
238000003776 cleavage reaction Methods 0.000 abstract description 2
238000003759 clinical diagnosis Methods 0.000 abstract description 2
229910052816 inorganic phosphate Inorganic materials 0.000 abstract description 2
230000007017 scission Effects 0.000 abstract description 2
229950006238 nadide Drugs 0.000 description 5
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 description 4
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
HXXFSFRBOHSIMQ-UHFFFAOYSA-N [3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl] dihydrogen phosphate Chemical compound OCC1OC(OP(O)(O)=O)C(O)C(O)C1O HXXFSFRBOHSIMQ-UHFFFAOYSA-N 0.000 description 4
239000008103 glucose Substances 0.000 description 4
238000004737 colorimetric analysis Methods 0.000 description 3
239000000203 mixture Substances 0.000 description 3
230000003647 oxidation Effects 0.000 description 3
238000007254 oxidation reaction Methods 0.000 description 3
230000035945 sensitivity Effects 0.000 description 3
238000012360 testing method Methods 0.000 description 3
XTUZNJKZDCNDAP-UHFFFAOYSA-N 1-[2-(4-iodophenyl)-3-nitrophenyl]-5-phenyl-2H-tetrazol-1-ium chloride Chemical compound [Cl-].[O-][N+](=O)C1=CC=CC([N+]2=C(N=NN2)C=2C=CC=CC=2)=C1C1=CC=C(I)C=C1 XTUZNJKZDCNDAP-UHFFFAOYSA-N 0.000 description 2
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 2
229920000945 Amylopectin Polymers 0.000 description 2
108091006149 Electron carriers Proteins 0.000 description 2
108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 description 2
102100022624 Glucoamylase Human genes 0.000 description 2
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 2
241000283973 Oryctolagus cuniculus Species 0.000 description 2
108010065081 Phosphorylase b Proteins 0.000 description 2
239000001177 diphosphate Substances 0.000 description 2
239000004615 ingredient Substances 0.000 description 2
210000003205 muscle Anatomy 0.000 description 2
239000008363 phosphate buffer Substances 0.000 description 2
239000011780 sodium chloride Substances 0.000 description 2
229920000856 Amylose Polymers 0.000 description 1
CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 1
101710088194 Dehydrogenase Proteins 0.000 description 1
229920001353 Dextrin Polymers 0.000 description 1
239000004375 Dextrin Substances 0.000 description 1
102000028526 Dihydrolipoamide Dehydrogenase Human genes 0.000 description 1
108010028127 Dihydrolipoamide Dehydrogenase Proteins 0.000 description 1
229920001503 Glucan Polymers 0.000 description 1
229920002527 Glycogen Polymers 0.000 description 1
229920002774 Maltodextrin Polymers 0.000 description 1
239000005913 Maltodextrin Substances 0.000 description 1
102100026367 Pancreatic alpha-amylase Human genes 0.000 description 1
108010065084 Phosphorylase a Proteins 0.000 description 1
238000013459 approach Methods 0.000 description 1
210000001124 body fluid Anatomy 0.000 description 1
239000010839 body fluid Substances 0.000 description 1
238000007398 colorimetric assay Methods 0.000 description 1
238000001514 detection method Methods 0.000 description 1
235000019425 dextrin Nutrition 0.000 description 1
XPPKVPWEQAFLFU-UHFFFAOYSA-J diphosphate(4-) Chemical compound [O-]P([O-])(=O)OP([O-])([O-])=O XPPKVPWEQAFLFU-UHFFFAOYSA-J 0.000 description 1
235000011180 diphosphates Nutrition 0.000 description 1
230000002255 enzymatic effect Effects 0.000 description 1
-1 glucose-l-phosphate Glucose-l-phosphate phospho Chemical class 0.000 description 1
229940096919 glycogen Drugs 0.000 description 1
230000003301 hydrolyzing effect Effects 0.000 description 1
229910052740 iodine Inorganic materials 0.000 description 1
239000011630 iodine Substances 0.000 description 1
229940035034 maltodextrin Drugs 0.000 description 1
108010085781 maltodextrin phosphorylase Proteins 0.000 description 1
238000012986 modification Methods 0.000 description 1
230000004048 modification Effects 0.000 description 1
229920001542 oligosaccharide Polymers 0.000 description 1
150000002482 oligosaccharides Chemical class 0.000 description 1
210000000056 organ Anatomy 0.000 description 1
210000000496 pancreas Anatomy 0.000 description 1
KHIWWQKSHDUIBK-UHFFFAOYSA-N periodic acid Chemical compound OI(=O)(=O)=O KHIWWQKSHDUIBK-UHFFFAOYSA-N 0.000 description 1
230000009467 reduction Effects 0.000 description 1
150000003839 salts Chemical class 0.000 description 1
239000012279 sodium borohydride Substances 0.000 description 1
229910000033 sodium borohydride Inorganic materials 0.000 description 1
235000000346 sugar Nutrition 0.000 description 1
150000008163 sugars Chemical class 0.000 description 1
239000000725 suspension Substances 0.000 description 1
125000003831 tetrazolyl group Chemical group 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

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)
Immunology (AREA)
Physics & Mathematics (AREA)
Molecular Biology (AREA)
Biotechnology (AREA)
Biophysics (AREA)
Analytical Chemistry (AREA)
Biochemistry (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)

CA281,158A 1976-07-01 1977-06-22 DOSAGE DE L'ACTIVITE DE L'.alpha.-AMYLASE SUR UN SUBSTRAT D'AMIDON MODIFIE Expired CA1068586A (fr)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
US70177876A	1976-07-01	1976-07-01

Publications (1)

Publication Number	Publication Date
CA1068586A true CA1068586A (fr)	1979-12-25

Family

ID=24818638

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
CA281,158A Expired CA1068586A (fr)	1976-07-01	1977-06-22	DOSAGE DE L'ACTIVITE DE L'.alpha.-AMYLASE SUR UN SUBSTRAT D'AMIDON MODIFIE

Country Status (5)

Country	Link
JP (1)	JPS533891A (fr)
CA (1)	CA1068586A (fr)
DE (1)	DE2729636B2 (fr)
FR (1)	FR2356939A1 (fr)
GB (1)	GB1543130A (fr)

Families Citing this family (5)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US4304854A (en)	1978-06-06	1981-12-08	Worthington Biochemical Corporation	Alpha-amylase assay and substrates for use therein
EP0048035B1 (fr) *	1978-06-06	1983-12-07	Flow General, Inc.	Maltodextrine phosphorylase dextrine limite et procédé pour sa préparation
JPS5768798A (en) *	1980-10-14	1982-04-27	Toyo Jozo Co Ltd	Novel measurement of amylase activity
US4649108A (en) *	1984-07-26	1987-03-10	Genzyme Corporation	Alpha amylase assay
US5043436A (en) *	1986-11-20	1991-08-27	Kurita Water Ind., Ltd.	Substrate for measurement of alpha-amylase activity

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CA973499A (en) *	1970-07-28	1975-08-26	Hayashibara, Ken	Process for the preparation of amylose as the substrate for the quantitative analysis of amylose
US3879263A (en) *	1973-09-06	1975-04-22	Du Pont	Method for the determination of amylase
US4097336A (en) *	1976-02-13	1978-06-27	Beckman Instruments, Inc.	Reagent system for beta-amylase assay

1977
- 1977-06-22 CA CA281,158A patent/CA1068586A/fr not_active Expired
- 1977-06-29 JP JP7668477A patent/JPS533891A/ja active Granted
- 1977-06-30 FR FR7720191A patent/FR2356939A1/fr active Granted
- 1977-06-30 GB GB2751577A patent/GB1543130A/en not_active Expired
- 1977-06-30 DE DE19772729636 patent/DE2729636B2/de not_active Ceased

Also Published As

Publication number	Publication date
FR2356939A1 (fr)	1978-01-27
GB1543130A (en)	1979-03-28
JPS533891A (en)	1978-01-13
JPS5639637B2 (fr)	1981-09-14
DE2729636A1 (de)	1978-02-02
DE2729636B2 (de)	1979-03-15
FR2356939B1 (fr)	1983-11-25

Publication	Publication Date	Title
Self	1985	Enzyme amplification—a general method applied to provide an immunoassisted assay for placental alkaline phosphatase
Zajoncová et al.	2004	A biosensor for the determination of amylase activity
McCleary	1980	New chromogenic substrates for the assay of alpha-amylase and (1→ 4)-β-d-glucanase
US4036697A (en)	1977-07-19	Kinetic assay for alpha-amylase
US4547280A (en)	1985-10-15	Maltose sensor
CA1068586A (fr)	1979-12-25	DOSAGE DE L'ACTIVITE DE L'.alpha.-AMYLASE SUR UN SUBSTRAT D'AMIDON MODIFIE
CA1076935A (fr)	1980-05-06	Essai cynetique pour l'alpha-amylase
Ogbomo et al.	1991	Flow-injection systems for the determination of oxidoreductase substrates: applications in food quality control and process monitoring
US4550077A (en)	1985-10-29	β-Amylase determination
US4304854A (en)	1981-12-08	Alpha-amylase assay and substrates for use therein
US4505756A (en)	1985-03-19	Alpha-amylase assay and substrates for use therein
Jones	1979	An enzymic microassay for starch
Krisman et al.	1985	Branching enzyme assay: selective quantitation of the α1, 6-linked glucosyl residues involved in the branching points
US4162194A (en)	1979-07-24	Kinetic assay for acid phosphotase and composition therefore
EP0005867B1 (fr)	1982-10-27	Détermination de l'alpha-amylase, une composition réactive et une système réactive pour ladite détermination
JPS5931699A (ja)	1984-02-20	α−アミラ−ゼ活性の測定法
US4159923A (en)	1979-07-03	Kinetic assay for inorganic phosphates and composition therefore
JPS5913198B2 (ja)	1984-03-28	アミラ−ゼ活性測定方法
JPH083479B2 (ja)	1996-01-17	マルトオリゴ糖計測用酵素電極
US4395487A (en)	1983-07-26	Method for assay of α-amylase activity
JPH05123193A (ja)	1993-05-21	α−アミラーゼ活性の測定法およびα−アミラーゼ活性測定用試薬
Van Leeuwen	1979	New saccharogenic determination of alpha-amylase in serum and urine.
JPS5939300A (ja)	1984-03-03	α−アミラ−ゼ活性の測定方法
JPS606855A (ja)	1985-01-14	α−アミラ−ゼの定量方法
JP2738482B2 (ja)	1998-04-08	酵素的測定法