DE69320583T2 - Nachweis von Antibiotika - Google Patents
Nachweis von AntibiotikaInfo
- Publication number
- DE69320583T2 DE69320583T2 DE1993620583 DE69320583T DE69320583T2 DE 69320583 T2 DE69320583 T2 DE 69320583T2 DE 1993620583 DE1993620583 DE 1993620583 DE 69320583 T DE69320583 T DE 69320583T DE 69320583 T2 DE69320583 T2 DE 69320583T2
- Authority
- DE
- Germany
- Prior art keywords
- antibiotic
- binding protein
- immobilized
- labelled
- immobilised
- 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 - Lifetime
Links
- 239000003242 anti bacterial agent Substances 0.000 title claims description 24
- 238000001514 detection method Methods 0.000 title claims description 10
- 229940088710 antibiotic agent Drugs 0.000 title description 14
- 230000003115 biocidal effect Effects 0.000 claims description 88
- 238000012360 testing method Methods 0.000 claims description 47
- 238000000034 method Methods 0.000 claims description 37
- 102000014914 Carrier Proteins Human genes 0.000 claims description 35
- 108091008324 binding proteins Proteins 0.000 claims description 35
- 229940098773 bovine serum albumin Drugs 0.000 claims description 31
- 108091003079 Bovine Serum Albumin Proteins 0.000 claims description 28
- 102000004190 Enzymes Human genes 0.000 claims description 23
- 108090000790 Enzymes Proteins 0.000 claims description 23
- 239000007788 liquid Substances 0.000 claims description 16
- 150000003952 β-lactams Chemical class 0.000 claims description 14
- 239000008267 milk Substances 0.000 claims description 11
- 210000004080 milk Anatomy 0.000 claims description 11
- 235000013336 milk Nutrition 0.000 claims description 11
- CEAZRRDELHUEMR-URQXQFDESA-N Gentamicin Chemical compound O1[C@H](C(C)NC)CC[C@@H](N)[C@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](NC)[C@@](C)(O)CO2)O)[C@H](N)C[C@@H]1N CEAZRRDELHUEMR-URQXQFDESA-N 0.000 claims description 9
- 229930182566 Gentamicin Natural products 0.000 claims description 9
- 108010001336 Horseradish Peroxidase Proteins 0.000 claims description 9
- 239000007790 solid phase Substances 0.000 claims description 8
- 244000005700 microbiome Species 0.000 claims description 7
- 229960002518 gentamicin Drugs 0.000 claims description 6
- 238000006243 chemical reaction Methods 0.000 claims description 5
- 241000193385 Geobacillus stearothermophilus Species 0.000 claims description 4
- 210000004369 blood Anatomy 0.000 claims description 4
- 239000008280 blood Substances 0.000 claims description 4
- 150000001875 compounds Chemical class 0.000 claims description 4
- 210000002700 urine Anatomy 0.000 claims description 4
- 239000011324 bead Substances 0.000 claims description 3
- 239000011248 coating agent Substances 0.000 claims description 3
- 238000000576 coating method Methods 0.000 claims description 3
- 239000004098 Tetracycline Substances 0.000 claims description 2
- 238000001042 affinity chromatography Methods 0.000 claims description 2
- 239000012530 fluid Substances 0.000 claims description 2
- 239000007850 fluorescent dye Substances 0.000 claims description 2
- 102000013415 peroxidase activity proteins Human genes 0.000 claims description 2
- 108040007629 peroxidase activity proteins Proteins 0.000 claims description 2
- 235000019364 tetracycline Nutrition 0.000 claims description 2
- 150000003522 tetracyclines Chemical class 0.000 claims description 2
- 239000003795 chemical substances by application Substances 0.000 claims 1
- 229960002180 tetracycline Drugs 0.000 claims 1
- 229930101283 tetracycline Natural products 0.000 claims 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 22
- 229940088598 enzyme Drugs 0.000 description 22
- 239000000243 solution Substances 0.000 description 21
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 14
- 102000004169 proteins and genes Human genes 0.000 description 12
- 108090000623 proteins and genes Proteins 0.000 description 12
- 238000011534 incubation Methods 0.000 description 11
- 239000011780 sodium chloride Substances 0.000 description 11
- HAXFWIACAGNFHA-UHFFFAOYSA-N aldrithiol Chemical group C=1C=CC=NC=1SSC1=CC=CC=N1 HAXFWIACAGNFHA-UHFFFAOYSA-N 0.000 description 10
- 229910019142 PO4 Inorganic materials 0.000 description 9
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 9
- 239000010452 phosphate Substances 0.000 description 9
- 239000000758 substrate Substances 0.000 description 9
- 239000000872 buffer Substances 0.000 description 8
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 8
- 230000021615 conjugation Effects 0.000 description 7
- 238000002523 gelfiltration Methods 0.000 description 7
- 125000006850 spacer group Chemical group 0.000 description 7
- 229930182555 Penicillin Natural products 0.000 description 6
- 229920005654 Sephadex Polymers 0.000 description 6
- 239000012507 Sephadex™ Substances 0.000 description 6
- 239000000047 product Substances 0.000 description 6
- 239000011159 matrix material Substances 0.000 description 5
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- 229940049954 penicillin Drugs 0.000 description 5
- 239000011541 reaction mixture Substances 0.000 description 5
- 239000012064 sodium phosphate buffer Substances 0.000 description 5
- 239000012089 stop solution Substances 0.000 description 5
- 239000002253 acid Substances 0.000 description 4
- 210000004027 cell Anatomy 0.000 description 4
- 238000011161 development Methods 0.000 description 4
- 238000002372 labelling Methods 0.000 description 4
- 235000019371 penicillin G benzathine Nutrition 0.000 description 4
- 229940056360 penicillin g Drugs 0.000 description 4
- 238000005406 washing Methods 0.000 description 4
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 3
- 101710116957 D-alanyl-D-alanine carboxypeptidase Proteins 0.000 description 3
- XEKOWRVHYACXOJ-UHFFFAOYSA-N Ethyl acetate Chemical compound CCOC(C)=O XEKOWRVHYACXOJ-UHFFFAOYSA-N 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 239000003153 chemical reaction reagent Substances 0.000 description 3
- 239000003431 cross linking reagent Substances 0.000 description 3
- 238000000502 dialysis Methods 0.000 description 3
- 238000010790 dilution Methods 0.000 description 3
- 239000012895 dilution Substances 0.000 description 3
- 239000012153 distilled water Substances 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 239000002953 phosphate buffered saline Substances 0.000 description 3
- -1 sulfamethazine Chemical class 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 125000003396 thiol group Chemical group [H]S* 0.000 description 3
- JWDFQMWEFLOOED-UHFFFAOYSA-N (2,5-dioxopyrrolidin-1-yl) 3-(pyridin-2-yldisulfanyl)propanoate Chemical compound O=C1CCC(=O)N1OC(=O)CCSSC1=CC=CC=N1 JWDFQMWEFLOOED-UHFFFAOYSA-N 0.000 description 2
- QMXCRMQIVATQMR-UHFFFAOYSA-N (2,5-dioxopyrrolidin-1-yl) 3-pyridin-2-ylsulfanylpropanoate Chemical compound O=C1CCC(=O)N1OC(=O)CCSC1=CC=CC=N1 QMXCRMQIVATQMR-UHFFFAOYSA-N 0.000 description 2
- 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 2
- RLFWWDJHLFCNIJ-UHFFFAOYSA-N 4-aminoantipyrine Chemical compound CN1C(C)=C(N)C(=O)N1C1=CC=CC=C1 RLFWWDJHLFCNIJ-UHFFFAOYSA-N 0.000 description 2
- HSHGZXNAXBPPDL-HZGVNTEJSA-N 7beta-aminocephalosporanic acid Chemical compound S1CC(COC(=O)C)=C(C([O-])=O)N2C(=O)[C@@H]([NH3+])[C@@H]12 HSHGZXNAXBPPDL-HZGVNTEJSA-N 0.000 description 2
- 229930186147 Cephalosporin Natural products 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 239000004793 Polystyrene Substances 0.000 description 2
- 239000013504 Triton X-100 Substances 0.000 description 2
- 229920004890 Triton X-100 Polymers 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- 229940124587 cephalosporin Drugs 0.000 description 2
- 150000001780 cephalosporins Chemical class 0.000 description 2
- 238000010382 chemical cross-linking Methods 0.000 description 2
- 238000010168 coupling process Methods 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
- 239000003480 eluent Substances 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 2
- 238000003018 immunoassay Methods 0.000 description 2
- 239000006166 lysate Substances 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 229910052760 oxygen Inorganic materials 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 239000004033 plastic Substances 0.000 description 2
- 229920003023 plastic Polymers 0.000 description 2
- 229920002223 polystyrene Polymers 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- JQWHASGSAFIOCM-UHFFFAOYSA-M sodium periodate Chemical compound [Na+].[O-]I(=O)(=O)=O JQWHASGSAFIOCM-UHFFFAOYSA-M 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 150000003573 thiols Chemical class 0.000 description 2
- XPFJYKARVSSRHE-UHFFFAOYSA-K trisodium;2-hydroxypropane-1,2,3-tricarboxylate;2-hydroxypropane-1,2,3-tricarboxylic acid Chemical compound [Na+].[Na+].[Na+].OC(=O)CC(O)(C(O)=O)CC(O)=O.[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O XPFJYKARVSSRHE-UHFFFAOYSA-K 0.000 description 2
- 238000002211 ultraviolet spectrum Methods 0.000 description 2
- GEYOCULIXLDCMW-UHFFFAOYSA-N 1,2-phenylenediamine Chemical compound NC1=CC=CC=C1N GEYOCULIXLDCMW-UHFFFAOYSA-N 0.000 description 1
- 238000005160 1H NMR spectroscopy Methods 0.000 description 1
- OBYNJKLOYWCXEP-UHFFFAOYSA-N 2-[3-(dimethylamino)-6-dimethylazaniumylidenexanthen-9-yl]-4-isothiocyanatobenzoate Chemical compound C=12C=CC(=[N+](C)C)C=C2OC2=CC(N(C)C)=CC=C2C=1C1=CC(N=C=S)=CC=C1C([O-])=O OBYNJKLOYWCXEP-UHFFFAOYSA-N 0.000 description 1
- YRNWIFYIFSBPAU-UHFFFAOYSA-N 4-[4-(dimethylamino)phenyl]-n,n-dimethylaniline Chemical compound C1=CC(N(C)C)=CC=C1C1=CC=C(N(C)C)C=C1 YRNWIFYIFSBPAU-UHFFFAOYSA-N 0.000 description 1
- NVIAYEIXYQCDAN-CLZZGJSISA-N 7beta-aminodeacetoxycephalosporanic acid Chemical compound S1CC(C)=C(C(O)=O)N2C(=O)[C@@H](N)[C@@H]12 NVIAYEIXYQCDAN-CLZZGJSISA-N 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- UQLLWWBDSUHNEB-CZUORRHYSA-N Cefaprin Chemical compound N([C@H]1[C@@H]2N(C1=O)C(=C(CS2)COC(=O)C)C(O)=O)C(=O)CSC1=CC=NC=C1 UQLLWWBDSUHNEB-CZUORRHYSA-N 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- AVXURJPOCDRRFD-UHFFFAOYSA-N Hydroxylamine Chemical compound ON AVXURJPOCDRRFD-UHFFFAOYSA-N 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 101000582398 Staphylococcus aureus Replication initiation protein Proteins 0.000 description 1
- 241000194020 Streptococcus thermophilus Species 0.000 description 1
- 229930006000 Sucrose Natural products 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
- 238000005411 Van der Waals force Methods 0.000 description 1
- 239000002250 absorbent Substances 0.000 description 1
- 230000002745 absorbent Effects 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- LSQZJLSUYDQPKJ-NJBDSQKTSA-N amoxicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=C(O)C=C1 LSQZJLSUYDQPKJ-NJBDSQKTSA-N 0.000 description 1
- 229960003022 amoxicillin Drugs 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 229960000686 benzalkonium chloride Drugs 0.000 description 1
- CADWTSSKOVRVJC-UHFFFAOYSA-N benzyl(dimethyl)azanium;chloride Chemical compound [Cl-].C[NH+](C)CC1=CC=CC=C1 CADWTSSKOVRVJC-UHFFFAOYSA-N 0.000 description 1
- 239000003782 beta lactam antibiotic agent Substances 0.000 description 1
- 102000005936 beta-Galactosidase Human genes 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 230000001588 bifunctional effect Effects 0.000 description 1
- 238000010170 biological method Methods 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- VYLDEYYOISNGST-UHFFFAOYSA-N bissulfosuccinimidyl suberate Chemical compound O=C1C(S(=O)(=O)O)CC(=O)N1OC(=O)CCCCCCC(=O)ON1C(=O)C(S(O)(=O)=O)CC1=O VYLDEYYOISNGST-UHFFFAOYSA-N 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 229960004350 cefapirin Drugs 0.000 description 1
- ZBHXIWJRIFEVQY-IHMPYVIRSA-N ceftiofur Chemical compound S([C@@H]1[C@@H](C(N1C=1C(O)=O)=O)NC(=O)\C(=N/OC)C=2N=C(N)SC=2)CC=1CSC(=O)C1=CC=CO1 ZBHXIWJRIFEVQY-IHMPYVIRSA-N 0.000 description 1
- 229960005229 ceftiofur Drugs 0.000 description 1
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- 238000005859 coupling reaction Methods 0.000 description 1
- 238000003977 dairy farming Methods 0.000 description 1
- 230000008021 deposition Effects 0.000 description 1
- 229940061607 dibasic sodium phosphate Drugs 0.000 description 1
- FRTGEIHSCHXMTI-UHFFFAOYSA-N dimethyl octanediimidate Chemical compound COC(=N)CCCCCCC(=N)OC FRTGEIHSCHXMTI-UHFFFAOYSA-N 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 1
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- LSQZJLSUYDQPKJ-UHFFFAOYSA-N p-Hydroxyampicillin Natural products O=C1N2C(C(O)=O)C(C)(C)SC2C1NC(=O)C(N)C1=CC=C(O)C=C1 LSQZJLSUYDQPKJ-UHFFFAOYSA-N 0.000 description 1
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- 229960002135 sulfadimidine Drugs 0.000 description 1
- ASWVTGNCAZCNNR-UHFFFAOYSA-N sulfamethazine Chemical compound CC1=CC(C)=NC(NS(=O)(=O)C=2C=CC(N)=CC=2)=N1 ASWVTGNCAZCNNR-UHFFFAOYSA-N 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 239000008399 tap water Substances 0.000 description 1
- 235000020679 tap water Nutrition 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- 229940040944 tetracyclines Drugs 0.000 description 1
- JGVWCANSWKRBCS-UHFFFAOYSA-N tetramethylrhodamine thiocyanate Chemical compound [Cl-].C=12C=CC(N(C)C)=CC2=[O+]C2=CC(N(C)C)=CC=C2C=1C1=CC=C(SC#N)C=C1C(O)=O JGVWCANSWKRBCS-UHFFFAOYSA-N 0.000 description 1
- RTKIYNMVFMVABJ-UHFFFAOYSA-L thimerosal Chemical compound [Na+].CC[Hg]SC1=CC=CC=C1C([O-])=O RTKIYNMVFMVABJ-UHFFFAOYSA-L 0.000 description 1
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- 238000000108 ultra-filtration Methods 0.000 description 1
- 239000011240 wet gel Substances 0.000 description 1
- 239000002132 β-lactam antibiotic Substances 0.000 description 1
- 229940124586 β-lactam antibiotics Drugs 0.000 description 1
Landscapes
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Claims (18)
1. Verfahren zum Nachweis von mindestens einem Antibiotikum
in einem flüssigen Medium, das Stufen umfaßt, in denen
(a) eine Fluidprobe eines flüssigen Mediums, mindestens ein
markiertes antibiotisches Bindungsprotein, das von einem
antibiotisch empfindlichen Mikroorganismus erhältlich
ist, und mindestens ein immobilisiertes Antibiotikum
zusammengebracht werden,
(b) dem markierten antibiotischen Bindungsprotein ermöglicht
wird, sich an das immobilisierte Antibiotikum zu binden,
(c) das markierte antibiotische Bindungsprotein, das an das
immobilisierte Antibiotikum nicht gebunden ist, entfernt
wird und
(d) die Menge des markierten antibiotischen
Bindungsproteins, die an das immobilisierte Antibiotikum
gebunden ist, bestimmt wird.
2. Verfahren nach Anspruch 1, worin das flüssige Medium
Milch, Urin oder Blut ist.
3. Verfahren nach Anspruch 1 oder 2, worin die Stufe (a)
Maßnahmen enthält, gemäß welchen das markierte
antibiotische Bindungsprotein in Kontakt mit der
flüssigen Probe gebracht wird, dem Antibiotikum in der
Probe ermöglicht wird, mit dem markierten antibiotischen
Bindungsprotein eine Bindung einzugehen und nachfolgend
immobilisierte Antibiotikum zugegeben wird.
4. Verfahren nach einem der vorhergehenden Ansprüche, worin
das immobilisierte Antibiotikum mit jenem, das in der
flüssigen Probe vorliegt, identisch ist.
5. Verfahren nach einem der Ansprüche 1, 2 oder 3, worin
das immobilisierte Antibiotikum von jenem, das in der
flüssigen Probe vorliegt, verschieden ist.
6. Verfahren nach einem der vorhergehenden Ansprüche, worin
das immobilisierte Antibiotikum mindestens einer der
Stoffe β-Lactam, Tetracyclin, Sulfaverbindung und
Gentamycin ist.
7. Verfahren nach einem der vorhergehenden Ansprüche, worin
das immobilisierte Antibiotikum auf einem Teströhrchen,
einem Meßstab, einer Platte oder Kugeln immobilisiert
ist.
8. Verfahren nach einem der vorhergehenden Ansprüche, worin
das immobilisierte Antibiotikum ein β-Lactam-Spacer-
Protein-Konjugat ist.
9. Verfahren nach einem der vorhergehenden Ansprüche, worin
das immobilisierte Antibiotikum durch Rinderserumalbumin
(BSA) an eine feste Phase gebunden ist.
10. Verfahren nach einem der vorhergehenden Ansprüche, worin
das antibiotische Bindungsprotein von einem Stamm von
Bacillus stearothermophilus erhalten wird.
11. Verfahren nach einem der vorhergehenden Ansprüche, worin
die Markierung ein Enzym, vorzugsweise eine Peroxidase,
insbesondere eine Meerrettich-Peroxidase, ist.
12. Verfahren nach Anspruch 11, worin die Stufe (d) die
Maßnahme umfaßt, bei der dem enzymmarkierten
antibiotischen Bindungsprotein ermöglicht wird, eine
Reaktion zu katalysieren oder eine Reaktion zu hemmen.
13. Verfahren nach einem der Ansprüche 1 bis 10, worin die
Markierung eine Fluoreszenzverbindung ist.
14. Verfahren nach einem der vorhergehenden Ansprüche, worin
das antibiotische Bindungsprotein durch
Affinitätschromatographie erhalten wird.
15. Anordnung zum Durchführen des Verfahrens gemäß einem der
vorhergehenden Ansprüche, die mindestens ein markiertes
antibiotisches Bindungsprotein und mindestens ein
immobilisierte Antibiotikum enthält.
16. Behälter mit einer Innenbeschichtung aus einem
immobilisierten Antibiotikum zur Verwendung in dem
Verfahren nach einem der Ansprüche 1 bis 14 oder in der
Anordnung nach Anspruch 15.
17. Behälter nach Anspruch 16, worin das Antibiotikum an der
Innenoberfläche des Behälters mittels eines
Verknüpfungsmittels immobilisiert ist.
18. Antibiotikum-BSA-Konjugat, ausgewählt aus der Gruppe,
die aus 7ACA-Spacer-BSA und N-Pentadecakis-[N-(4-
carbonyl-3-methylceph-3-em-7-yl)-aminocarbonylethyl-
dithioethylcarbonyl]-BSA besteht.
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
EP92203084 | 1992-10-06 |
Publications (2)
Publication Number | Publication Date |
---|---|
DE69320583D1 DE69320583D1 (de) | 1998-10-01 |
DE69320583T2 true DE69320583T2 (de) | 1999-01-14 |
Family
ID=8210952
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
DE1993620583 Expired - Lifetime DE69320583T2 (de) | 1992-10-06 | 1993-09-24 | Nachweis von Antibiotika |
Country Status (6)
Country | Link |
---|---|
JP (1) | JPH06207936A (de) |
AT (1) | ATE170292T1 (de) |
AU (1) | AU662656B2 (de) |
CA (2) | CA2655875C (de) |
DE (1) | DE69320583T2 (de) |
NZ (1) | NZ248864A (de) |
Families Citing this family (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
KR102000202B1 (ko) * | 2015-11-20 | 2019-07-15 | 센트리언트 파마슈티칼스 네덜란드 비.브이. | 폐기물 내의 항생제의 결정을 위한 검정 |
JP2021189080A (ja) * | 2020-06-02 | 2021-12-13 | 公立大学法人福島県立医科大学 | 化合物を基板上に固定する方法および固定化した化合物の検出方法 |
Family Cites Families (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4239852A (en) * | 1978-06-12 | 1980-12-16 | Penicillin Assays, Inc. | Antibiotic detection method |
US4347312A (en) * | 1980-03-20 | 1982-08-31 | Research Triangle Institute | Detection of antibiotics in milk |
-
1993
- 1993-09-24 DE DE1993620583 patent/DE69320583T2/de not_active Expired - Lifetime
- 1993-09-24 AT AT93202754T patent/ATE170292T1/de not_active IP Right Cessation
- 1993-10-05 AU AU48792/93A patent/AU662656B2/en not_active Expired
- 1993-10-05 NZ NZ24886493A patent/NZ248864A/en not_active IP Right Cessation
- 1993-10-06 JP JP25027493A patent/JPH06207936A/ja active Pending
- 1993-10-06 CA CA2655875A patent/CA2655875C/en not_active Expired - Lifetime
- 1993-10-06 CA CA 2107856 patent/CA2107856C/en not_active Expired - Lifetime
Also Published As
Publication number | Publication date |
---|---|
CA2107856A1 (en) | 1994-04-07 |
CA2107856C (en) | 2009-04-28 |
CA2655875A1 (en) | 1994-04-07 |
AU662656B2 (en) | 1995-09-07 |
AU4879293A (en) | 1994-04-21 |
NZ248864A (en) | 1994-10-26 |
DE69320583D1 (de) | 1998-10-01 |
CA2655875C (en) | 2010-07-20 |
JPH06207936A (ja) | 1994-07-26 |
ATE170292T1 (de) | 1998-09-15 |
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