CA2183573A1 - Dispositif de calibrage/controle d'isoenzymes - Google Patents
Dispositif de calibrage/controle d'isoenzymesInfo
- Publication number
- CA2183573A1 CA2183573A1 CA 2183573 CA2183573A CA2183573A1 CA 2183573 A1 CA2183573 A1 CA 2183573A1 CA 2183573 CA2183573 CA 2183573 CA 2183573 A CA2183573 A CA 2183573A CA 2183573 A1 CA2183573 A1 CA 2183573A1
- Authority
- CA
- Canada
- Prior art keywords
- buffer
- isoenzyme
- free
- serum
- salt
- 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.)
- Abandoned
Links
- 108010044467 Isoenzymes Proteins 0.000 title claims abstract description 68
- 239000000872 buffer Substances 0.000 claims abstract description 55
- 239000000203 mixture Substances 0.000 claims abstract description 38
- 238000003860 storage Methods 0.000 claims abstract description 38
- 239000012062 aqueous buffer Substances 0.000 claims abstract description 22
- 150000003839 salts Chemical class 0.000 claims abstract description 20
- 108010010803 Gelatin Proteins 0.000 claims abstract description 19
- 229920000159 gelatin Polymers 0.000 claims abstract description 19
- 235000019322 gelatine Nutrition 0.000 claims abstract description 19
- 235000011852 gelatine desserts Nutrition 0.000 claims abstract description 19
- 230000007774 longterm Effects 0.000 claims abstract description 19
- 239000008273 gelatin Substances 0.000 claims abstract description 17
- 239000002736 nonionic surfactant Substances 0.000 claims abstract description 17
- 239000003963 antioxidant agent Substances 0.000 claims abstract description 16
- 235000000346 sugar Nutrition 0.000 claims abstract description 16
- 230000003078 antioxidant effect Effects 0.000 claims abstract description 15
- 239000006174 pH buffer Substances 0.000 claims abstract description 14
- 229920001059 synthetic polymer Polymers 0.000 claims abstract description 13
- 238000007496 glass forming Methods 0.000 claims abstract description 8
- 238000010494 dissociation reaction Methods 0.000 claims abstract description 4
- 230000005593 dissociations Effects 0.000 claims abstract description 4
- 230000008707 rearrangement Effects 0.000 claims abstract description 4
- 230000000087 stabilizing effect Effects 0.000 claims description 27
- 238000000034 method Methods 0.000 claims description 24
- 239000007788 liquid Substances 0.000 claims description 15
- 239000007864 aqueous solution Substances 0.000 claims description 4
- 150000002772 monosaccharides Chemical class 0.000 claims description 4
- 239000000243 solution Substances 0.000 claims description 4
- 238000011033 desalting Methods 0.000 claims description 3
- 150000002840 non-reducing disaccharides Chemical class 0.000 claims description 2
- 150000003267 reducing disaccharides Chemical class 0.000 claims description 2
- GZCWLCBFPRFLKL-UHFFFAOYSA-N 1-prop-2-ynoxypropan-2-ol Chemical compound CC(O)COCC#C GZCWLCBFPRFLKL-UHFFFAOYSA-N 0.000 claims 6
- 102000013563 Acid Phosphatase Human genes 0.000 claims 6
- 108010051457 Acid Phosphatase Proteins 0.000 claims 6
- 102000002260 Alkaline Phosphatase Human genes 0.000 claims 6
- 108020004774 Alkaline Phosphatase Proteins 0.000 claims 6
- 239000004382 Amylase Substances 0.000 claims 6
- 102000003846 Carbonic anhydrases Human genes 0.000 claims 6
- 108090000209 Carbonic anhydrases Proteins 0.000 claims 6
- 108090000322 Cholinesterases Proteins 0.000 claims 6
- 102000003914 Cholinesterases Human genes 0.000 claims 6
- 102000004420 Creatine Kinase Human genes 0.000 claims 6
- 108010042126 Creatine kinase Proteins 0.000 claims 6
- 102000003855 L-lactate dehydrogenase Human genes 0.000 claims 6
- 108700023483 L-lactate dehydrogenases Proteins 0.000 claims 6
- 102000002704 Leucyl aminopeptidase Human genes 0.000 claims 6
- 108010004098 Leucyl aminopeptidase Proteins 0.000 claims 6
- 102000004882 Lipase Human genes 0.000 claims 6
- 108090001060 Lipase Proteins 0.000 claims 6
- 239000004367 Lipase Substances 0.000 claims 6
- 102000004357 Transferases Human genes 0.000 claims 6
- 108090000992 Transferases Proteins 0.000 claims 6
- 229940048961 cholinesterase Drugs 0.000 claims 6
- 235000019421 lipase Nutrition 0.000 claims 6
- 102000004625 Aspartate Aminotransferases Human genes 0.000 claims 5
- 108010003415 Aspartate Aminotransferases Proteins 0.000 claims 5
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims 1
- 229940009098 aspartate Drugs 0.000 claims 1
- 210000002966 serum Anatomy 0.000 abstract description 19
- 238000009472 formulation Methods 0.000 abstract description 17
- 230000000694 effects Effects 0.000 abstract description 16
- 238000001035 drying Methods 0.000 abstract description 6
- 230000001900 immune effect Effects 0.000 abstract description 5
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 33
- 229920001213 Polysorbate 20 Polymers 0.000 description 13
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 13
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 13
- 230000002255 enzymatic effect Effects 0.000 description 10
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 8
- 239000007995 HEPES buffer Substances 0.000 description 8
- PXIPVTKHYLBLMZ-UHFFFAOYSA-N Sodium azide Chemical compound [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 description 8
- 239000003795 chemical substances by application Substances 0.000 description 7
- 238000003556 assay Methods 0.000 description 6
- URDCARMUOSMFFI-UHFFFAOYSA-N 2-[2-[bis(carboxymethyl)amino]ethyl-(2-hydroxyethyl)amino]acetic acid Chemical compound OCCN(CC(O)=O)CCN(CC(O)=O)CC(O)=O URDCARMUOSMFFI-UHFFFAOYSA-N 0.000 description 5
- PWKSKIMOESPYIA-BYPYZUCNSA-N L-N-acetyl-Cysteine Chemical compound CC(=O)N[C@@H](CS)C(O)=O PWKSKIMOESPYIA-BYPYZUCNSA-N 0.000 description 5
- 229960004308 acetylcysteine Drugs 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 238000011084 recovery Methods 0.000 description 5
- 108090000790 Enzymes Proteins 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000623 proteins and genes Proteins 0.000 description 4
- 102000004169 proteins and genes Human genes 0.000 description 4
- 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 3
- 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 3
- 239000000427 antigen Substances 0.000 description 3
- 102000036639 antigens Human genes 0.000 description 3
- 108091007433 antigens Proteins 0.000 description 3
- 238000011109 contamination Methods 0.000 description 3
- 238000011026 diafiltration Methods 0.000 description 3
- 201000010099 disease Diseases 0.000 description 3
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 3
- -1 monosaccharide sugars Chemical class 0.000 description 3
- 229920000036 polyvinylpyrrolidone Polymers 0.000 description 3
- 239000001267 polyvinylpyrrolidone Substances 0.000 description 3
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- SRBFZHDQGSBBOR-IOVATXLUSA-N D-xylopyranose Chemical compound O[C@@H]1COC(O)[C@H](O)[C@H]1O SRBFZHDQGSBBOR-IOVATXLUSA-N 0.000 description 2
- ZTHYODDOHIVTJV-UHFFFAOYSA-N Propyl gallate Chemical compound CCCOC(=O)C1=CC(O)=C(O)C(O)=C1 ZTHYODDOHIVTJV-UHFFFAOYSA-N 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 206010000891 acute myocardial infarction Diseases 0.000 description 2
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 2
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 2
- 239000002738 chelating agent Substances 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 239000003638 chemical reducing agent Substances 0.000 description 2
- CVSVTCORWBXHQV-UHFFFAOYSA-N creatine Chemical compound NC(=[NH2+])N(C)CC([O-])=O CVSVTCORWBXHQV-UHFFFAOYSA-N 0.000 description 2
- 150000002016 disaccharides Chemical class 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
- 230000002163 immunogen Effects 0.000 description 2
- 230000005847 immunogenicity Effects 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- HCZKYJDFEPMADG-TXEJJXNPSA-N masoprocol Chemical compound C([C@H](C)[C@H](C)CC=1C=C(O)C(O)=CC=1)C1=CC=C(O)C(O)=C1 HCZKYJDFEPMADG-TXEJJXNPSA-N 0.000 description 2
- 229910052751 metal Inorganic materials 0.000 description 2
- 239000002184 metal Substances 0.000 description 2
- 239000003755 preservative agent Substances 0.000 description 2
- 239000012925 reference material Substances 0.000 description 2
- 238000005070 sampling Methods 0.000 description 2
- UMGDCJDMYOKAJW-UHFFFAOYSA-N thiourea Chemical compound NC(N)=S UMGDCJDMYOKAJW-UHFFFAOYSA-N 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- HDTRYLNUVZCQOY-UHFFFAOYSA-N α-D-glucopyranosyl-α-D-glucopyranoside Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(O)C(O)C(CO)O1 HDTRYLNUVZCQOY-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
- IEQAICDLOKRSRL-UHFFFAOYSA-N 2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-[2-(2-dodecoxyethoxy)ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethanol Chemical compound CCCCCCCCCCCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCOCCO IEQAICDLOKRSRL-UHFFFAOYSA-N 0.000 description 1
- GUQMDNQYMMRJPY-UHFFFAOYSA-N 4,4-dimethyl-1,3-oxazolidine Chemical compound CC1(C)COCN1 GUQMDNQYMMRJPY-UHFFFAOYSA-N 0.000 description 1
- QYYMDNHUJFIDDQ-UHFFFAOYSA-N 5-chloro-2-methyl-1,2-thiazol-3-one;2-methyl-1,2-thiazol-3-one Chemical compound CN1SC=CC1=O.CN1SC(Cl)=CC1=O QYYMDNHUJFIDDQ-UHFFFAOYSA-N 0.000 description 1
- 241000251468 Actinopterygii Species 0.000 description 1
- GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose 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-XLOQQCSPSA-N 0.000 description 1
- GUBGYTABKSRVRQ-CUHNMECISA-N D-Cellobiose 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)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-CUHNMECISA-N 0.000 description 1
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 1
- 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 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 229930091371 Fructose Natural products 0.000 description 1
- 239000005715 Fructose Substances 0.000 description 1
- 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 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
- 108010024636 Glutathione Proteins 0.000 description 1
- 229920001612 Hydroxyethyl starch Polymers 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 239000007990 PIPES buffer Substances 0.000 description 1
- 108091000080 Phosphotransferase Proteins 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- MUPFEKGTMRGPLJ-RMMQSMQOSA-N Raffinose Natural products O(C[C@H]1[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O[C@@]2(CO)[C@H](O)[C@@H](O)[C@@H](CO)O2)O1)[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 MUPFEKGTMRGPLJ-RMMQSMQOSA-N 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- HDTRYLNUVZCQOY-WSWWMNSNSA-N Trehalose Natural products O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-WSWWMNSNSA-N 0.000 description 1
- MUPFEKGTMRGPLJ-UHFFFAOYSA-N UNPD196149 Natural products OC1C(O)C(CO)OC1(CO)OC1C(O)C(O)C(O)C(COC2C(C(O)C(O)C(CO)O2)O)O1 MUPFEKGTMRGPLJ-UHFFFAOYSA-N 0.000 description 1
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Natural products NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 1
- HDTRYLNUVZCQOY-LIZSDCNHSA-N alpha,alpha-trehalose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-LIZSDCNHSA-N 0.000 description 1
- WQZGKKKJIJFFOK-PHYPRBDBSA-N alpha-D-galactose Chemical compound OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-PHYPRBDBSA-N 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 229940053200 antiepileptics fatty acid derivative Drugs 0.000 description 1
- PYMYPHUHKUWMLA-WDCZJNDASA-N arabinose Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)C=O PYMYPHUHKUWMLA-WDCZJNDASA-N 0.000 description 1
- 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 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
- 229960003624 creatine Drugs 0.000 description 1
- 239000006046 creatine Substances 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000008021 deposition Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 239000002532 enzyme inhibitor Substances 0.000 description 1
- HCZKYJDFEPMADG-UHFFFAOYSA-N erythro-nordihydroguaiaretic acid Natural products C=1C=C(O)C(O)=CC=1CC(C)C(C)CC1=CC=C(O)C(O)=C1 HCZKYJDFEPMADG-UHFFFAOYSA-N 0.000 description 1
- DEFVIWRASFVYLL-UHFFFAOYSA-N ethylene glycol bis(2-aminoethyl)tetraacetic acid Chemical compound OC(=O)CN(CC(O)=O)CCOCCOCCN(CC(O)=O)CC(O)=O DEFVIWRASFVYLL-UHFFFAOYSA-N 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 229930182830 galactose Natural products 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 239000000383 hazardous chemical Substances 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- IPCSVZSSVZVIGE-UHFFFAOYSA-M hexadecanoate Chemical compound CCCCCCCCCCCCCCCC([O-])=O IPCSVZSSVZVIGE-UHFFFAOYSA-M 0.000 description 1
- DNZMDASEFMLYBU-RNBXVSKKSA-N hydroxyethyl starch Chemical compound OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@@H]1O.OCCOC[C@H]1O[C@H](OCCO)[C@H](OCCO)[C@@H](OCCO)[C@@H]1OCCO DNZMDASEFMLYBU-RNBXVSKKSA-N 0.000 description 1
- 229940050526 hydroxyethylstarch Drugs 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 230000000984 immunochemical effect Effects 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 238000012417 linear regression Methods 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 229960003951 masoprocol Drugs 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 230000002107 myocardial effect Effects 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- OQICDZLCHORSMX-UHFFFAOYSA-N oxirane-2,2,3-triol Chemical compound OC1OC1(O)O OQICDZLCHORSMX-UHFFFAOYSA-N 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 102000020233 phosphotransferase Human genes 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 229920000053 polysorbate 80 Polymers 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- 239000000473 propyl gallate Substances 0.000 description 1
- 229940075579 propyl gallate Drugs 0.000 description 1
- 235000010388 propyl gallate Nutrition 0.000 description 1
- MUPFEKGTMRGPLJ-ZQSKZDJDSA-N raffinose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO[C@@H]2[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O2)O)O1 MUPFEKGTMRGPLJ-ZQSKZDJDSA-N 0.000 description 1
- 159000000000 sodium salts Chemical class 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 235000013311 vegetables Nutrition 0.000 description 1
- 229920002554 vinyl polymer Polymers 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/96—Stabilising an enzyme by forming an adduct or a composition; Forming enzyme conjugates
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Enzymes And Modification Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Medicinal Preparation (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Abstract
L'invention concerne des tampons utilisés pour stabiliser les isoenzymes à l'aide de formulations qui, après séchage et reconstitution, recouvrent la quasi-totalité de l'activité isoenzymatique et de la masse immunologique pour une longue durée de conservation, sans dissociation ni réarrangement de leurs sous-unités. Le tampon utilisé pendant le long stockage à sec de l'isoenzyme est un tampon aqueux exempt de sérum et de sels, comprenant 1) un sucre vitrifiant, 2) un mélange antioxydant, 3) un tampon pH et 4) un tensioactif non ionique et/ou un polymère synthétique et/ou une gélatine. Le tampon utilisé pour la reconstitution d'un échantillon enzymatique sans sérum et sans sel comprend un tampon aqueux à teneur en sel. L'invention porte également sur un isoenzyme sérique comprenant 1) un tampon pH, 2) un sel, 3) un mélange antioxydant et 4) un tensioactif non ionique et/ou un polymère synthétique et/ou une gélatine. La figure montre la stabilisation accélérée de la masse enzymatique dans un tampon aqueux avec du sérum et dans un tampon aqueux sans sérum, déterminée à l'aide d'un graphique d'Arrhénius, représentant le nombre de jours nécessaires à une stabilisation, en relation inverse avec la température, pour extrapoler une conservation de longue durée à 5 ~C.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US19891994A | 1994-02-18 | 1994-02-18 | |
| US08/198,919 | 1994-02-18 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2183573A1 true CA2183573A1 (fr) | 1995-08-24 |
Family
ID=22735444
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA 2183573 Abandoned CA2183573A1 (fr) | 1994-02-18 | 1995-02-17 | Dispositif de calibrage/controle d'isoenzymes |
Country Status (5)
| Country | Link |
|---|---|
| EP (1) | EP0751989A4 (fr) |
| JP (1) | JPH09509064A (fr) |
| AU (1) | AU700666B2 (fr) |
| CA (1) | CA2183573A1 (fr) |
| WO (1) | WO1995022602A1 (fr) |
Families Citing this family (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7074581B2 (en) * | 2002-08-09 | 2006-07-11 | Sysmex Corporation | Reagent for assaying lipid |
| CN102628863B (zh) * | 2012-04-19 | 2016-05-11 | 上海蓝怡科技有限公司 | 标记了碱性磷酸酶抗原抗体稀释液 |
| DK3234563T3 (da) | 2014-12-18 | 2025-02-10 | Radiometer Medical Aps | Fremgangsmåde til kalibrering af en indretning til måling af koncentrationen af kreatinin |
| EP4530635A3 (fr) | 2014-12-18 | 2025-06-25 | Radiometer Medical ApS | Nouveaux procédés d'étalonnage |
| CN109298193A (zh) * | 2018-09-25 | 2019-02-01 | 山东博科生物产业有限公司 | 一种稳定性强的生化检测用液态心肌酶谱复合质控品 |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4883762A (en) * | 1983-06-06 | 1989-11-28 | Ciba Corning Diagnostics Corp. | Stabilized isoenzyme control products |
| US5059341A (en) * | 1989-03-16 | 1991-10-22 | Olin Corporation | Cleaning composition comprising microbial lipase SD2, sodium dodecylbenzene sulfonate and gelatin |
-
1995
- 1995-02-17 CA CA 2183573 patent/CA2183573A1/fr not_active Abandoned
- 1995-02-17 JP JP7521896A patent/JPH09509064A/ja active Pending
- 1995-02-17 WO PCT/US1995/001927 patent/WO1995022602A1/fr not_active Ceased
- 1995-02-17 EP EP95910271A patent/EP0751989A4/fr not_active Withdrawn
- 1995-02-17 AU AU18448/95A patent/AU700666B2/en not_active Ceased
Also Published As
| Publication number | Publication date |
|---|---|
| WO1995022602A1 (fr) | 1995-08-24 |
| AU700666B2 (en) | 1999-01-14 |
| AU1844895A (en) | 1995-09-04 |
| EP0751989A4 (fr) | 1999-07-14 |
| EP0751989A1 (fr) | 1997-01-08 |
| JPH09509064A (ja) | 1997-09-16 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US5240843A (en) | Enzyme stabilisation | |
| US5348852A (en) | Diagnostic and therapeutic compositions | |
| JP3068836B2 (ja) | 物質の貯蔵 | |
| CA2040815C (fr) | Methode de stabilisation des enzymes | |
| US20170202954A1 (en) | Stabilization of Aqueous Compositions of Proteins With Displacement Buffers | |
| FI93494B (fi) | Menetelmä veren hyytymistekijöiden stabiloimiseksi | |
| JP2004505024A (ja) | 生物学的物質用の保存及び貯蔵媒体 | |
| US4931392A (en) | Process for stabilizing kinase | |
| JP3125610B2 (ja) | L−メチオニン γ−リアーゼの安定化法 | |
| Soliman et al. | Factors affecting freezing damage of lactic dehydrogenase | |
| EP0791658B1 (fr) | Composition enzymatique pour examen clinique | |
| AU700666B2 (en) | Isoenzyme calibrator/control products | |
| US5270194A (en) | Stabilized glucose oxidase from Aspergillus Niger | |
| JP2930277B2 (ja) | クレアチンキナーゼおよびクレアチンキナーゼイソ酵素の酵素活性および免疫反応性を安定させるための組成物 | |
| US4339533A (en) | Stabilization of creatine kinase (CK) and its application as a reference standard | |
| CA1102225A (fr) | Compose liquide stabilise contenant une enzyme et une coenzyme et methode de preparation | |
| JP3696267B2 (ja) | 生理活性蛋白質の安定化方法 | |
| CA1226794A (fr) | Produit de controle stabilise multiparametre | |
| JPS59166084A (ja) | 安定な酵素試薬の製造法 | |
| JP5425062B2 (ja) | D−マンニトールを含有する管理試料を用いるグリコアルブミン等の測定方法 | |
| EP0418940B1 (fr) | Stabilisation de l'enzyme glucose-oxydase en réactif liquide | |
| JP2008206491A (ja) | p−ヒドロキシ安息香酸水酸化酵素の安定化方法 | |
| JP4288559B2 (ja) | アスコルビン酸オキシダーゼの安定化方法および安定化組成物 | |
| JPS62111686A (ja) | 安定なグアナ−ゼ組成物 | |
| JPH0640824B2 (ja) | 安定なフラクト−スデヒドロゲナ−ゼ組成物 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FZDE | Dead |