JPH0332357B2 - - Google Patents

Info

Publication number: JPH0332357B2
Authority: JP; Japan
Prior art keywords: enzyme; immobilized; creatine; enzymes; creatinine
Prior art date: 1982-03-18
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 - Lifetime

Application number

JP57044191A

Other languages

English (en)

Japanese (ja)

Other versions

JPS58162294A (ja

Inventor

Toshio Tsuchida

Kentaro Yoda

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.)

Toyobo Co Ltd

Original Assignee

Toyobo Co Ltd

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.)

1982-03-18

Filing date

1982-03-18

Publication date

1991-05-10

1982-03-18 Application filed by Toyobo Co Ltd filed Critical Toyobo Co Ltd

1982-03-18 Priority to JP57044191A priority Critical patent/JPS58162294A/ja

1983-09-26 Publication of JPS58162294A publication Critical patent/JPS58162294A/ja

1991-05-10 Publication of JPH0332357B2 publication Critical patent/JPH0332357B2/ja

Status Granted legal-status Critical Current

Links

102000004190 Enzymes Human genes 0.000 claims description 84
108090000790 Enzymes Proteins 0.000 claims description 84
239000002131 composite material Substances 0.000 claims description 21
229910052751 metal Inorganic materials 0.000 claims description 13
239000002184 metal Substances 0.000 claims description 13
239000002738 chelating agent Substances 0.000 claims description 10
239000003638 chemical reducing agent Substances 0.000 claims description 10
239000000872 buffer Substances 0.000 claims description 8
239000000203 mixture Substances 0.000 claims description 8
229940088598 enzyme Drugs 0.000 description 88
CVSVTCORWBXHQV-UHFFFAOYSA-N creatine Chemical compound NC(=[NH2+])N(C)CC([O-])=O CVSVTCORWBXHQV-UHFFFAOYSA-N 0.000 description 38
DDRJAANPRJIHGJ-UHFFFAOYSA-N creatinine Chemical compound CN1CC(=O)NC1=N DDRJAANPRJIHGJ-UHFFFAOYSA-N 0.000 description 34
229960003624 creatine Drugs 0.000 description 19
239000006046 creatine Substances 0.000 description 19
229940109239 creatinine Drugs 0.000 description 17
MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 15
239000012528 membrane Substances 0.000 description 15
238000000034 method Methods 0.000 description 12
230000000694 effects Effects 0.000 description 11
239000003381 stabilizer Substances 0.000 description 10
239000007853 buffer solution Substances 0.000 description 8
238000005259 measurement Methods 0.000 description 7
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 6
DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 6
239000003153 chemical reaction reagent Substances 0.000 description 6
238000010586 diagram Methods 0.000 description 6
239000000126 substance Substances 0.000 description 6
108010077078 Creatinase Proteins 0.000 description 5
108010060059 Sarcosine Oxidase Proteins 0.000 description 5
102000008118 Sarcosine oxidase Human genes 0.000 description 5
238000006243 chemical reaction Methods 0.000 description 5
238000004737 colorimetric analysis Methods 0.000 description 5
PXIPVTKHYLBLMZ-UHFFFAOYSA-N Sodium azide Chemical compound [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 description 4
239000012190 activator Substances 0.000 description 4
-1 ammonium ions Chemical class 0.000 description 4
230000003100 immobilizing effect Effects 0.000 description 4
230000003647 oxidation Effects 0.000 description 4
238000007254 oxidation reaction Methods 0.000 description 4
239000008057 potassium phosphate buffer Substances 0.000 description 4
FSYKKLYZXJSNPZ-UHFFFAOYSA-N sarcosine Chemical compound C[NH2+]CC([O-])=O FSYKKLYZXJSNPZ-UHFFFAOYSA-N 0.000 description 4
108010066906 Creatininase Proteins 0.000 description 3
WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 3
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
239000004471 Glycine Substances 0.000 description 3
108090000854 Oxidoreductases Proteins 0.000 description 3
102000004316 Oxidoreductases Human genes 0.000 description 3
229940081735 acetylcellulose Drugs 0.000 description 3
239000011324 bead Substances 0.000 description 3
238000004364 calculation method Methods 0.000 description 3
229920002301 cellulose acetate Polymers 0.000 description 3
238000001514 detection method Methods 0.000 description 3
239000000243 solution Substances 0.000 description 3
KWSLGOVYXMQPPX-UHFFFAOYSA-N 5-[3-(trifluoromethyl)phenyl]-2h-tetrazole Chemical compound FC(F)(F)C1=CC=CC(C2=NNN=N2)=C1 KWSLGOVYXMQPPX-UHFFFAOYSA-N 0.000 description 2
108091003079 Bovine Serum Albumin Proteins 0.000 description 2
229920001661 Chitosan Polymers 0.000 description 2
SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 2
108010024636 Glutathione Proteins 0.000 description 2
108010093096 Immobilized Enzymes Proteins 0.000 description 2
XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 2
PXHVJJICTQNCMI-UHFFFAOYSA-N Nickel Chemical compound [Ni] PXHVJJICTQNCMI-UHFFFAOYSA-N 0.000 description 2
108010077895 Sarcosine Proteins 0.000 description 2
XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
SMEGJBVQLJJKKX-HOTMZDKISA-N [(2R,3S,4S,5R,6R)-5-acetyloxy-3,4,6-trihydroxyoxan-2-yl]methyl acetate Chemical compound CC(=O)OC[C@@H]1[C@H]([C@@H]([C@H]([C@@H](O1)O)OC(=O)C)O)O SMEGJBVQLJJKKX-HOTMZDKISA-N 0.000 description 2
210000004369 blood Anatomy 0.000 description 2
239000008280 blood Substances 0.000 description 2
210000001124 body fluid Anatomy 0.000 description 2
239000010839 body fluid Substances 0.000 description 2
229940098773 bovine serum albumin Drugs 0.000 description 2
HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 2
238000004040 coloring Methods 0.000 description 2
150000001875 compounds Chemical class 0.000 description 2
VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 2
238000003411 electrode reaction Methods 0.000 description 2
230000002255 enzymatic effect Effects 0.000 description 2
DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 2
239000000835 fiber Substances 0.000 description 2
RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 2
239000012510 hollow fiber Substances 0.000 description 2
230000000977 initiatory effect Effects 0.000 description 2
239000011777 magnesium Substances 0.000 description 2
ACVYVLVWPXVTIT-UHFFFAOYSA-N phosphinic acid Chemical compound O[PH2]=O ACVYVLVWPXVTIT-UHFFFAOYSA-N 0.000 description 2
239000000843 powder Substances 0.000 description 2
150000003839 salts Chemical class 0.000 description 2
229940043230 sarcosine Drugs 0.000 description 2
230000035945 sensitivity Effects 0.000 description 2
210000002966 serum Anatomy 0.000 description 2
229910001379 sodium hypophosphite Inorganic materials 0.000 description 2
ISIJQEHRDSCQIU-UHFFFAOYSA-N tert-butyl 2,7-diazaspiro[4.5]decane-7-carboxylate Chemical compound C1N(C(=O)OC(C)(C)C)CCCC11CNCC1 ISIJQEHRDSCQIU-UHFFFAOYSA-N 0.000 description 2
125000003396 thiol group Chemical group [H]S* 0.000 description 2
DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-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 1
102000008146 Acetate-CoA ligase Human genes 0.000 description 1
108010049926 Acetate-CoA ligase Proteins 0.000 description 1
ZSLZBFCDCINBPY-ZSJPKINUSA-N Acetyl-CoA Natural products O[C@@H]1[C@H](OP(O)(O)=O)[C@@H](COP(O)(=O)OP(O)(=O)OCC(C)(C)[C@@H](O)C(=O)NCCC(=O)NCCSC(=O)C)O[C@H]1N1C2=NC=NC(N)=C2N=C1 ZSLZBFCDCINBPY-ZSJPKINUSA-N 0.000 description 1
OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 description 1
108010089254 Cholesterol oxidase Proteins 0.000 description 1
102000008186 Collagen Human genes 0.000 description 1
108010035532 Collagen Proteins 0.000 description 1
RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 1
108010010803 Gelatin Proteins 0.000 description 1
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 1
102000057621 Glycerol kinases Human genes 0.000 description 1
FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
JLVVSXFLKOJNIY-UHFFFAOYSA-N Magnesium ion Chemical compound [Mg+2] JLVVSXFLKOJNIY-UHFFFAOYSA-N 0.000 description 1
102100024295 Maltase-glucoamylase Human genes 0.000 description 1
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 1
229910019142 PO4 Inorganic materials 0.000 description 1
239000004793 Polystyrene Substances 0.000 description 1
101710163410 Probable glycerol kinase Proteins 0.000 description 1
BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 1
108010055297 Sterol Esterase Proteins 0.000 description 1
102000000019 Sterol Esterase Human genes 0.000 description 1
239000007983 Tris buffer Substances 0.000 description 1
HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 description 1
238000002835 absorbance Methods 0.000 description 1
239000008351 acetate buffer Substances 0.000 description 1
229940100228 acetyl coenzyme a Drugs 0.000 description 1
230000004913 activation Effects 0.000 description 1
125000003172 aldehyde group Chemical group 0.000 description 1
102000004139 alpha-Amylases Human genes 0.000 description 1
108090000637 alpha-Amylases Proteins 0.000 description 1
108010028144 alpha-Glucosidases Proteins 0.000 description 1
229940024171 alpha-amylase Drugs 0.000 description 1
125000003277 amino group Chemical group 0.000 description 1
238000004458 analytical method Methods 0.000 description 1
239000007864 aqueous solution Substances 0.000 description 1
229910052788 barium Inorganic materials 0.000 description 1
DSAJWYNOEDNPEQ-UHFFFAOYSA-N barium atom Chemical compound [Ba] DSAJWYNOEDNPEQ-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
230000001588 bifunctional effect Effects 0.000 description 1
KGBXLFKZBHKPEV-UHFFFAOYSA-N boric acid Chemical compound OB(O)O KGBXLFKZBHKPEV-UHFFFAOYSA-N 0.000 description 1
239000004327 boric acid Substances 0.000 description 1
229910052793 cadmium Inorganic materials 0.000 description 1
BDOSMKKIYDKNTQ-UHFFFAOYSA-N cadmium atom Chemical compound [Cd] BDOSMKKIYDKNTQ-UHFFFAOYSA-N 0.000 description 1
229910052791 calcium Inorganic materials 0.000 description 1
239000011575 calcium Substances 0.000 description 1
229910001424 calcium ion Inorganic materials 0.000 description 1
239000004202 carbamide Substances 0.000 description 1
239000000969 carrier Substances 0.000 description 1
150000003943 catecholamines Chemical class 0.000 description 1
235000012000 cholesterol Nutrition 0.000 description 1
229940107161 cholesterol Drugs 0.000 description 1
239000010941 cobalt Substances 0.000 description 1
229910017052 cobalt Inorganic materials 0.000 description 1
GUTLYIVDDKVIGB-UHFFFAOYSA-N cobalt atom Chemical compound [Co] GUTLYIVDDKVIGB-UHFFFAOYSA-N 0.000 description 1
229920001436 collagen Polymers 0.000 description 1
230000000052 comparative effect Effects 0.000 description 1
238000001816 cooling Methods 0.000 description 1
229910052802 copper Inorganic materials 0.000 description 1
239000010949 copper Substances 0.000 description 1
238000004132 cross linking Methods 0.000 description 1
230000009849 deactivation Effects 0.000 description 1
SULWMEGSVQCTSK-UHFFFAOYSA-N diethyl hydrogen phosphite Chemical compound CCOP(O)OCC SULWMEGSVQCTSK-UHFFFAOYSA-N 0.000 description 1
238000011438 discrete method Methods 0.000 description 1
150000002148 esters Chemical class 0.000 description 1
QDHCHVWSKUMZDZ-UHFFFAOYSA-N ethyl dihydrogen phosphite Chemical compound CCOP(O)O QDHCHVWSKUMZDZ-UHFFFAOYSA-N 0.000 description 1
239000003925 fat Substances 0.000 description 1
229920000159 gelatin Polymers 0.000 description 1
239000008273 gelatin Substances 0.000 description 1
235000019322 gelatine Nutrition 0.000 description 1
235000011852 gelatine desserts Nutrition 0.000 description 1
238000001879 gelation Methods 0.000 description 1
239000011521 glass Substances 0.000 description 1
239000008103 glucose Substances 0.000 description 1
230000002452 interceptive effect Effects 0.000 description 1
150000002500 ions Chemical class 0.000 description 1
229910052742 iron Inorganic materials 0.000 description 1
229910052749 magnesium Inorganic materials 0.000 description 1
229910001425 magnesium ion Inorganic materials 0.000 description 1
229960002160 maltose Drugs 0.000 description 1
WPBNNNQJVZRUHP-UHFFFAOYSA-L manganese(2+);methyl n-[[2-(methoxycarbonylcarbamothioylamino)phenyl]carbamothioyl]carbamate;n-[2-(sulfidocarbothioylamino)ethyl]carbamodithioate Chemical compound [Mn+2].[S-]C(=S)NCCNC([S-])=S.COC(=O)NC(=S)NC1=CC=CC=C1NC(=S)NC(=O)OC WPBNNNQJVZRUHP-UHFFFAOYSA-L 0.000 description 1
QSHDDOUJBYECFT-UHFFFAOYSA-N mercury Chemical compound [Hg] QSHDDOUJBYECFT-UHFFFAOYSA-N 0.000 description 1
229910052753 mercury Inorganic materials 0.000 description 1
229910021645 metal ion Inorganic materials 0.000 description 1
150000002739 metals Chemical class 0.000 description 1
238000000465 moulding Methods 0.000 description 1
230000007935 neutral effect Effects 0.000 description 1
229910052759 nickel Inorganic materials 0.000 description 1
229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 1
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 1
239000010452 phosphate Substances 0.000 description 1
239000008363 phosphate buffer Substances 0.000 description 1
229920002401 polyacrylamide Polymers 0.000 description 1
239000004417 polycarbonate Substances 0.000 description 1
229920000515 polycarbonate Polymers 0.000 description 1
229920002223 polystyrene Polymers 0.000 description 1
239000005373 porous glass Substances 0.000 description 1
229910001414 potassium ion Inorganic materials 0.000 description 1
229910052709 silver Inorganic materials 0.000 description 1
239000004332 silver Substances 0.000 description 1
239000000758 substrate Substances 0.000 description 1
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
NCPXQVVMIXIKTN-UHFFFAOYSA-N trisodium;phosphite Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])[O-] NCPXQVVMIXIKTN-UHFFFAOYSA-N 0.000 description 1
235000021122 unsaturated fatty acids Nutrition 0.000 description 1
150000004670 unsaturated fatty acids Chemical class 0.000 description 1
210000002700 urine Anatomy 0.000 description 1
238000010200 validation analysis Methods 0.000 description 1
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
229910052725 zinc Inorganic materials 0.000 description 1
239000011701 zinc Substances 0.000 description 1

Landscapes

Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Enzymes And Modification Thereof (AREA)
Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)

JP57044191A 1982-03-18 1982-03-18 固定化複合酵素組成物 Granted JPS58162294A (ja)

Priority Applications (1)

Application Number	Priority Date	Filing Date	Title
JP57044191A JPS58162294A (ja)	1982-03-18	1982-03-18	固定化複合酵素組成物

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
JP57044191A JPS58162294A (ja)	1982-03-18	1982-03-18	固定化複合酵素組成物

Publications (2)

Publication Number	Publication Date
JPS58162294A JPS58162294A (ja)	1983-09-26
JPH0332357B2 true JPH0332357B2 (de)	1991-05-10

Family

ID=12684673

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
JP57044191A Granted JPS58162294A (ja)	1982-03-18	1982-03-18	固定化複合酵素組成物

Country Status (1)

Country	Link
JP (1)	JPS58162294A (de)

Families Citing this family (7)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
JPS62502653A (ja) *	1985-02-11	1987-10-15	トラベノ−ル‐ジエネンテツク、ダイアグノスチクス	安定化された酵素基質溶液
JPH07110240B2 (ja) *	1985-04-01	1995-11-29	小林製薬株式会社	クレアチニンアミドヒドロラーゼ製剤
US5217890A (en) *	1991-08-20	1993-06-08	Eastman Kodak Company	Stabilized composition containing creatine kinase and protein having blocked sulfhydryl groups
US20040256227A1 (en) *	2003-02-11	2004-12-23	Jungwon Shin	Electrochemical urea sensors and methods of making the same
US8268604B2 (en) *	2007-12-20	2012-09-18	Abbott Point Of Care Inc.	Compositions for forming immobilized biological layers for sensing
GB201002824D0 (en) *	2010-02-19	2010-04-07	Temasek Polytechnic	A method of preparing a substrate for immobilization of functional substances thereon and the substrate obtained therefrom
CN108140848B (zh) *	2015-07-15	2022-02-01	齐姆特罗尼克斯公司	自动化生物纳米催化剂生产

1982
- 1982-03-18 JP JP57044191A patent/JPS58162294A/ja active Granted

Also Published As

Publication number	Publication date
JPS58162294A (ja)	1983-09-26

Publication	Publication Date	Title
Cammann	1977	Bio-sensors based on ion-selective electrodes
Bertrand et al.	1981	Multipurpose electrode with different enzyme systems bound to collagen films
Meyerhoff et al.	1976	An activated enzyme electrode for creatinine
Guilbault et al.	1973	Enzyme electrodes for the determination of 1-phenylalanine
Khue et al.	1991	Immobilized enzyme electrode for creatinine determination in serum
US4780191A (en)	1988-10-25	L-glutamine sensor
Inman et al.	1974	Preparation of some immobilized linked enzyme systems and their use in the automated determination of disaccharides
US4234681A (en)	1980-11-18	Immobolized light emitting systems
Kauffmann et al.	1992	Enzyme electrode biosensors: theory and applications
Assolant-Vinet et al.	1987	A novel enzyme membrane electrode for oxalate determination in foodstuffs
Guilbault et al.	1979	Preparation and analytical uses of immobilized enzymes
Kobos	1980	Potentiometric enzyme methods
Matsumoto et al.	1980	Amperometric determination of choline with use of immobilized choline oxidase
JPH0332357B2 (de)	1991-05-10
Minh et al.	1978	Enzyme-bound thermistor as an enthalpimetric sensor
CA1109374A (en)	1981-09-22	Stabilization of activated galactose oxidase enzyme
Canh et al.	1979	Enzyme electrode for inhibitors determination: urease-fluoride system
Abdel-Latif et al.	1990	Fluorometric determination of urea by flow injection analysis
Neujahr	1984	Biosensors for environmental control
US4042462A (en)	1977-08-16	Creatine phosphokinase determination method
US4927752A (en)	1990-05-22	Support used in bioluminescent dosing of enzymes, substrates or enzymatic inhibitors
Mottola	1987	Enzymes as analytical reagents: substrate determinations with soluble and with immobilised enzyme preparations. Plenary lecture
Guilbault	1980	Enzyme electrode probes
Romette et al.	1987	L-glutamine enzyme electrode for on-line mammalian cell culture process control
Guilbault	1982	Immobilized enzymes as analytical reagents