AU2004269340B2 - Materials and methods for capture of pathogens and removal of aurintricarboxylic acid from a sample - Google Patents
Materials and methods for capture of pathogens and removal of aurintricarboxylic acid from a sample Download PDFInfo
- Publication number
- AU2004269340B2 AU2004269340B2 AU2004269340A AU2004269340A AU2004269340B2 AU 2004269340 B2 AU2004269340 B2 AU 2004269340B2 AU 2004269340 A AU2004269340 A AU 2004269340A AU 2004269340 A AU2004269340 A AU 2004269340A AU 2004269340 B2 AU2004269340 B2 AU 2004269340B2
- Authority
- AU
- Australia
- Prior art keywords
- sample
- composition
- urea
- nucleic acid
- blood
- 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.)
- Ceased
Links
- 238000000034 method Methods 0.000 title claims abstract description 83
- GIXWDMTZECRIJT-UHFFFAOYSA-N aurintricarboxylic acid Chemical compound C1=CC(=O)C(C(=O)O)=CC1=C(C=1C=C(C(O)=CC=1)C(O)=O)C1=CC=C(O)C(C(O)=O)=C1 GIXWDMTZECRIJT-UHFFFAOYSA-N 0.000 title claims abstract description 47
- 244000052769 pathogen Species 0.000 title description 39
- 239000000463 material Substances 0.000 title description 12
- 210000004369 blood Anatomy 0.000 claims abstract description 66
- 239000008280 blood Substances 0.000 claims abstract description 66
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 38
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 36
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 36
- 239000000203 mixture Substances 0.000 claims abstract description 30
- 238000000605 extraction Methods 0.000 claims abstract description 18
- 239000003153 chemical reaction reagent Substances 0.000 claims description 50
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims description 28
- 239000004202 carbamide Substances 0.000 claims description 28
- 241000894006 Bacteria Species 0.000 claims description 19
- 239000002245 particle Substances 0.000 claims description 18
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 18
- 108010067770 Endopeptidase K Proteins 0.000 claims description 16
- 150000003839 salts Chemical class 0.000 claims description 15
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims description 12
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 12
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 claims description 11
- 239000001509 sodium citrate Substances 0.000 claims description 9
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 claims description 9
- -1 N-heptylcarbamoyl Chemical group 0.000 claims description 8
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 claims description 6
- 108010046334 Urease Proteins 0.000 claims description 6
- 238000010438 heat treatment Methods 0.000 claims description 6
- 238000005406 washing Methods 0.000 claims description 6
- 239000000843 powder Substances 0.000 claims description 4
- 108010002069 Defensins Proteins 0.000 claims description 2
- 102000000541 Defensins Human genes 0.000 claims description 2
- 108700022013 Insecta cecropin B Proteins 0.000 claims description 2
- 108090001090 Lectins Proteins 0.000 claims description 2
- 102000004856 Lectins Human genes 0.000 claims description 2
- 108010007568 Protamines Proteins 0.000 claims description 2
- 102000007327 Protamines Human genes 0.000 claims description 2
- 101800003783 Tritrpticin Proteins 0.000 claims description 2
- 150000001408 amides Chemical class 0.000 claims description 2
- 150000001413 amino acids Chemical class 0.000 claims description 2
- 108010040767 buforin I Proteins 0.000 claims description 2
- 108010025307 buforin II Proteins 0.000 claims description 2
- 108010046237 cecropin P1-LI Proteins 0.000 claims description 2
- PRIVBYDFWSFUFP-RJLJEYQFSA-N cecropin p1 Chemical compound O=C([C@H](CCC(N)=O)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](C)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@@H](N)CO)[C@@H](C)O)[C@@H](C)CC)[C@@H](C)CC)NCC(=O)NCC(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCNC(N)=N)C(O)=O PRIVBYDFWSFUFP-RJLJEYQFSA-N 0.000 claims description 2
- UKVZSPHYQJNTOU-IVBHRGSNSA-N chembl1240717 Chemical compound C([C@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@@H](N)[C@H](C)O)CC(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCCN)C(O)=O)C1=CC=CC=C1 UKVZSPHYQJNTOU-IVBHRGSNSA-N 0.000 claims description 2
- 150000002148 esters Chemical class 0.000 claims description 2
- 239000002523 lectin Substances 0.000 claims description 2
- 230000004048 modification Effects 0.000 claims description 2
- 238000012986 modification Methods 0.000 claims description 2
- 229940048914 protamine Drugs 0.000 claims description 2
- FTKYRNHHOBRIOY-HQUBJAAMSA-N tritrptcin Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@@H](N)C(C)C)C1=CC=CC=C1 FTKYRNHHOBRIOY-HQUBJAAMSA-N 0.000 claims description 2
- QPCDCPDFJACHGM-UHFFFAOYSA-N N,N-bis{2-[bis(carboxymethyl)amino]ethyl}glycine Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(=O)O)CCN(CC(O)=O)CC(O)=O QPCDCPDFJACHGM-UHFFFAOYSA-N 0.000 claims 6
- WYMDDFRYORANCC-UHFFFAOYSA-N 2-[[3-[bis(carboxymethyl)amino]-2-hydroxypropyl]-(carboxymethyl)amino]acetic acid Chemical compound OC(=O)CN(CC(O)=O)CC(O)CN(CC(O)=O)CC(O)=O WYMDDFRYORANCC-UHFFFAOYSA-N 0.000 claims 2
- 229940071106 ethylenediaminetetraacetate Drugs 0.000 claims 2
- 101800003223 Cecropin-A Proteins 0.000 claims 1
- HCQPHKMLKXOJSR-IRCPFGJUSA-N cecropin-a Chemical compound C([C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)NCC(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(N)=O)[C@@H](C)CC)C(C)C)[C@@H](C)CC)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@@H](N)CCCCN)C1=CC=CC=C1 HCQPHKMLKXOJSR-IRCPFGJUSA-N 0.000 claims 1
- 230000003196 chaotropic effect Effects 0.000 claims 1
- 238000002955 isolation Methods 0.000 claims 1
- 239000007790 solid phase Substances 0.000 claims 1
- 102000016911 Deoxyribonucleases Human genes 0.000 abstract description 22
- 108010053770 Deoxyribonucleases Proteins 0.000 abstract description 22
- 102000004190 Enzymes Human genes 0.000 abstract description 22
- 108090000790 Enzymes Proteins 0.000 abstract description 21
- 210000000633 nuclear envelope Anatomy 0.000 abstract description 5
- 239000000523 sample Substances 0.000 description 56
- 102000009123 Fibrin Human genes 0.000 description 34
- 108010073385 Fibrin Proteins 0.000 description 34
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 34
- 229950003499 fibrin Drugs 0.000 description 34
- 102000013566 Plasminogen Human genes 0.000 description 32
- 108010051456 Plasminogen Proteins 0.000 description 32
- 230000009089 cytolysis Effects 0.000 description 30
- 108010023197 Streptokinase Proteins 0.000 description 25
- 229960005202 streptokinase Drugs 0.000 description 25
- 102100037611 Lysophospholipase Human genes 0.000 description 23
- 108010058864 Phospholipases A2 Proteins 0.000 description 23
- 229940088598 enzyme Drugs 0.000 description 21
- 108020004414 DNA Proteins 0.000 description 19
- 102100031780 Endonuclease Human genes 0.000 description 19
- 230000001717 pathogenic effect Effects 0.000 description 19
- 239000000243 solution Substances 0.000 description 18
- 108010042407 Endonucleases Proteins 0.000 description 17
- 239000000872 buffer Substances 0.000 description 17
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 16
- KIUKXJAPPMFGSW-DNGZLQJQSA-N (2S,3S,4S,5R,6R)-6-[(2S,3R,4R,5S,6R)-3-Acetamido-2-[(2S,3S,4R,5R,6R)-6-[(2R,3R,4R,5S,6R)-3-acetamido-2,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-2-carboxy-4,5-dihydroxyoxan-3-yl]oxy-5-hydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-3,4,5-trihydroxyoxane-2-carboxylic acid Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[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]3[C@@H]([C@@H](O)[C@H](O)[C@H](O3)C(O)=O)O)[C@H](O)[C@@H](CO)O2)NC(C)=O)[C@@H](C(O)=O)O1 KIUKXJAPPMFGSW-DNGZLQJQSA-N 0.000 description 15
- 238000006243 chemical reaction Methods 0.000 description 15
- 229920002674 hyaluronan Polymers 0.000 description 15
- 229960003160 hyaluronic acid Drugs 0.000 description 15
- QPCDCPDFJACHGM-UHFFFAOYSA-K pentetate(3-) Chemical compound OC(=O)CN(CC([O-])=O)CCN(CC([O-])=O)CCN(CC(O)=O)CC([O-])=O QPCDCPDFJACHGM-UHFFFAOYSA-K 0.000 description 15
- LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 14
- 238000004458 analytical method Methods 0.000 description 13
- 230000000975 bioactive effect Effects 0.000 description 13
- 238000003752 polymerase chain reaction Methods 0.000 description 13
- 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 12
- 238000012360 testing method Methods 0.000 description 12
- 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 11
- 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 11
- 241000700605 Viruses Species 0.000 description 11
- 239000008188 pellet Substances 0.000 description 11
- 102000004882 Lipase Human genes 0.000 description 10
- 108090001060 Lipase Proteins 0.000 description 10
- 239000004367 Lipase Substances 0.000 description 10
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 10
- 239000003599 detergent Substances 0.000 description 10
- 238000007710 freezing Methods 0.000 description 10
- 235000019421 lipase Nutrition 0.000 description 10
- 229920004890 Triton X-100 Polymers 0.000 description 9
- 239000013504 Triton X-100 Substances 0.000 description 9
- 238000001514 detection method Methods 0.000 description 9
- 241000894007 species Species 0.000 description 9
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 8
- 241000193738 Bacillus anthracis Species 0.000 description 8
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 8
- 230000001580 bacterial effect Effects 0.000 description 8
- 239000000306 component Substances 0.000 description 8
- 201000010099 disease Diseases 0.000 description 8
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 8
- 230000008014 freezing Effects 0.000 description 8
- 239000011159 matrix material Substances 0.000 description 8
- 230000008569 process Effects 0.000 description 8
- 239000011780 sodium chloride Substances 0.000 description 8
- 239000003053 toxin Substances 0.000 description 8
- 231100000765 toxin Toxicity 0.000 description 8
- 108700012359 toxins Proteins 0.000 description 8
- 229940065181 bacillus anthracis Drugs 0.000 description 7
- 239000000284 extract Substances 0.000 description 7
- 230000002779 inactivation Effects 0.000 description 7
- 229910000160 potassium phosphate Inorganic materials 0.000 description 7
- 235000011009 potassium phosphates Nutrition 0.000 description 7
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 6
- 108091000054 Prion Proteins 0.000 description 6
- 102000029797 Prion Human genes 0.000 description 6
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 6
- 108010090804 Streptavidin Proteins 0.000 description 6
- 238000000137 annealing Methods 0.000 description 6
- 238000005119 centrifugation Methods 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- 229940012957 plasmin Drugs 0.000 description 6
- 239000001397 quillaja saponaria molina bark Substances 0.000 description 6
- 229930182490 saponin Natural products 0.000 description 6
- 150000007949 saponins Chemical class 0.000 description 6
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 5
- 238000007400 DNA extraction Methods 0.000 description 5
- 108010049003 Fibrinogen Proteins 0.000 description 5
- 102000008946 Fibrinogen Human genes 0.000 description 5
- 241000233866 Fungi Species 0.000 description 5
- 241000607479 Yersinia pestis Species 0.000 description 5
- 239000011575 calcium Substances 0.000 description 5
- 229910052791 calcium Inorganic materials 0.000 description 5
- 150000001768 cations Chemical class 0.000 description 5
- 210000004027 cell Anatomy 0.000 description 5
- 230000029087 digestion Effects 0.000 description 5
- 229940012952 fibrinogen Drugs 0.000 description 5
- 238000001914 filtration Methods 0.000 description 5
- 239000012634 fragment Substances 0.000 description 5
- 238000002360 preparation method Methods 0.000 description 5
- 238000012340 reverse transcriptase PCR Methods 0.000 description 5
- 239000000377 silicon dioxide Substances 0.000 description 5
- 238000011282 treatment Methods 0.000 description 5
- 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 4
- 239000007995 HEPES buffer Substances 0.000 description 4
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 4
- 239000012491 analyte Substances 0.000 description 4
- 229960002685 biotin Drugs 0.000 description 4
- 235000020958 biotin Nutrition 0.000 description 4
- 239000011616 biotin Substances 0.000 description 4
- 239000007853 buffer solution Substances 0.000 description 4
- 239000013043 chemical agent Substances 0.000 description 4
- 210000002816 gill Anatomy 0.000 description 4
- 239000012139 lysis buffer Substances 0.000 description 4
- 239000011777 magnesium Substances 0.000 description 4
- 229910052749 magnesium Inorganic materials 0.000 description 4
- 229910001629 magnesium chloride Inorganic materials 0.000 description 4
- 238000004949 mass spectrometry Methods 0.000 description 4
- 230000002503 metabolic effect Effects 0.000 description 4
- 230000007065 protein hydrolysis Effects 0.000 description 4
- 239000003161 ribonuclease inhibitor Substances 0.000 description 4
- 239000012266 salt solution Substances 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- 239000006228 supernatant Substances 0.000 description 4
- 241000304886 Bacilli Species 0.000 description 3
- 108020000946 Bacterial DNA Proteins 0.000 description 3
- 102000007260 Deoxyribonuclease I Human genes 0.000 description 3
- 108010008532 Deoxyribonuclease I Proteins 0.000 description 3
- 101710163270 Nuclease Proteins 0.000 description 3
- 101710141795 Ribonuclease inhibitor Proteins 0.000 description 3
- 229940122208 Ribonuclease inhibitor Drugs 0.000 description 3
- 102100037968 Ribonuclease inhibitor Human genes 0.000 description 3
- XPIVOYOQXKNYHA-RGDJUOJXSA-N [(2r,3s,4s,5r,6s)-3,4,5-trihydroxy-6-methoxyoxan-2-yl]methyl n-heptylcarbamate Chemical compound CCCCCCCNC(=O)OC[C@H]1O[C@H](OC)[C@H](O)[C@@H](O)[C@@H]1O XPIVOYOQXKNYHA-RGDJUOJXSA-N 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 230000007717 exclusion Effects 0.000 description 3
- 238000009396 hybridization Methods 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 208000015181 infectious disease Diseases 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 238000002156 mixing Methods 0.000 description 3
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 3
- 230000003389 potentiating effect Effects 0.000 description 3
- 235000018102 proteins Nutrition 0.000 description 3
- 102000004169 proteins and genes Human genes 0.000 description 3
- 108090000623 proteins and genes Proteins 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- 239000012536 storage buffer Substances 0.000 description 3
- 238000010257 thawing Methods 0.000 description 3
- 210000001519 tissue Anatomy 0.000 description 3
- 208000031729 Bacteremia Diseases 0.000 description 2
- 108010003272 Hyaluronate lyase Proteins 0.000 description 2
- 102000001974 Hyaluronidases Human genes 0.000 description 2
- 108091028043 Nucleic acid sequence Proteins 0.000 description 2
- 206010035148 Plague Diseases 0.000 description 2
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 2
- 229930006000 Sucrose Natural products 0.000 description 2
- 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 2
- 238000013459 approach Methods 0.000 description 2
- 238000009640 blood culture Methods 0.000 description 2
- 230000030833 cell death Effects 0.000 description 2
- 239000012141 concentrate Substances 0.000 description 2
- 230000006378 damage Effects 0.000 description 2
- 238000000502 dialysis 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
- YQOKLYTXVFAUCW-UHFFFAOYSA-N guanidine;isothiocyanic acid Chemical compound N=C=S.NC(N)=N YQOKLYTXVFAUCW-UHFFFAOYSA-N 0.000 description 2
- ZJYYHGLJYGJLLN-UHFFFAOYSA-N guanidinium thiocyanate Chemical compound SC#N.NC(N)=N ZJYYHGLJYGJLLN-UHFFFAOYSA-N 0.000 description 2
- 229960002773 hyaluronidase Drugs 0.000 description 2
- 230000002458 infectious effect Effects 0.000 description 2
- 208000023372 inhalational anthrax Diseases 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 238000004895 liquid chromatography mass spectrometry Methods 0.000 description 2
- 239000006166 lysate Substances 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 230000002906 microbiologic effect Effects 0.000 description 2
- 239000002086 nanomaterial Substances 0.000 description 2
- 150000003904 phospholipids Chemical class 0.000 description 2
- 201000009430 pneumonic plague Diseases 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 239000011347 resin Substances 0.000 description 2
- 229920005989 resin Polymers 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- 239000011734 sodium Substances 0.000 description 2
- 239000005720 sucrose Substances 0.000 description 2
- 208000024891 symptom Diseases 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- 241000251468 Actinopterygii Species 0.000 description 1
- 239000002028 Biomass Substances 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 206010008479 Chest Pain Diseases 0.000 description 1
- 206010011224 Cough Diseases 0.000 description 1
- 239000004971 Cross linker Substances 0.000 description 1
- 230000007064 DNA hydrolysis Effects 0.000 description 1
- 208000000059 Dyspnea Diseases 0.000 description 1
- 206010013975 Dyspnoeas Diseases 0.000 description 1
- 206010022004 Influenza like illness Diseases 0.000 description 1
- 241000274177 Juniperus sabina Species 0.000 description 1
- 108010063045 Lactoferrin Proteins 0.000 description 1
- 102100032241 Lactotransferrin Human genes 0.000 description 1
- 241001460678 Napo <wasp> Species 0.000 description 1
- 238000002944 PCR assay Methods 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 208000000474 Poliomyelitis Diseases 0.000 description 1
- 239000004642 Polyimide Substances 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- 206010037660 Pyrexia Diseases 0.000 description 1
- 238000002123 RNA extraction Methods 0.000 description 1
- 206010040047 Sepsis Diseases 0.000 description 1
- 108090000190 Thrombin Proteins 0.000 description 1
- 108020005202 Viral DNA Proteins 0.000 description 1
- 101500009721 Xenopus laevis Magainin-2 Proteins 0.000 description 1
- 101000996404 Yersinia pestis Glutamine synthetase adenylyl transferase Proteins 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 238000003916 acid precipitation Methods 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- 102000036639 antigens Human genes 0.000 description 1
- 244000052616 bacterial pathogen Species 0.000 description 1
- 239000012148 binding buffer Substances 0.000 description 1
- 239000012472 biological sample Substances 0.000 description 1
- 239000000090 biomarker Substances 0.000 description 1
- 230000023555 blood coagulation Effects 0.000 description 1
- 239000012503 blood component Substances 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 150000001732 carboxylic acid derivatives Chemical class 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 230000009920 chelation Effects 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 239000003431 cross linking reagent Substances 0.000 description 1
- 230000034994 death Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 210000003743 erythrocyte Anatomy 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 229910052737 gold Inorganic materials 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 230000009545 invasion Effects 0.000 description 1
- CSSYQJWUGATIHM-IKGCZBKSSA-N l-phenylalanyl-l-lysyl-l-cysteinyl-l-arginyl-l-arginyl-l-tryptophyl-l-glutaminyl-l-tryptophyl-l-arginyl-l-methionyl-l-lysyl-l-lysyl-l-leucylglycyl-l-alanyl-l-prolyl-l-seryl-l-isoleucyl-l-threonyl-l-cysteinyl-l-valyl-l-arginyl-l-arginyl-l-alanyl-l-phenylal Chemical compound C([C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CS)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)C1=CC=CC=C1 CSSYQJWUGATIHM-IKGCZBKSSA-N 0.000 description 1
- 229940078795 lactoferrin Drugs 0.000 description 1
- 235000021242 lactoferrin Nutrition 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 238000004811 liquid chromatography Methods 0.000 description 1
- 238000001459 lithography Methods 0.000 description 1
- MGIUUAHJVPPFEV-ABXDCCGRSA-N magainin ii Chemical compound C([C@H](NC(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(O)=O)C1=CC=CC=C1 MGIUUAHJVPPFEV-ABXDCCGRSA-N 0.000 description 1
- 206010025482 malaise Diseases 0.000 description 1
- 201000001231 mediastinitis Diseases 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 229910000000 metal hydroxide Inorganic materials 0.000 description 1
- 150000004692 metal hydroxides Chemical class 0.000 description 1
- 150000002739 metals Chemical class 0.000 description 1
- 108091005601 modified peptides Proteins 0.000 description 1
- 229920000344 molecularly imprinted polymer Polymers 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 238000003499 nucleic acid array Methods 0.000 description 1
- 229920002113 octoxynol Polymers 0.000 description 1
- 239000013610 patient sample Substances 0.000 description 1
- 210000005259 peripheral blood Anatomy 0.000 description 1
- 239000011886 peripheral blood Substances 0.000 description 1
- 230000003836 peripheral circulation Effects 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 229940085991 phosphate ion Drugs 0.000 description 1
- 238000007747 plating Methods 0.000 description 1
- 229910052697 platinum Inorganic materials 0.000 description 1
- 229920001721 polyimide Polymers 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 238000010839 reverse transcription Methods 0.000 description 1
- 238000004062 sedimentation Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 208000013220 shortness of breath Diseases 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 229960004072 thrombin Drugs 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K17/00—Carrier-bound or immobilised peptides; Preparation thereof
- C07K17/02—Peptides being immobilised on, or in, an organic carrier
- C07K17/10—Peptides being immobilised on, or in, an organic carrier the carrier being a carbohydrate
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07C—ACYCLIC OR CARBOCYCLIC COMPOUNDS
- C07C51/00—Preparation of carboxylic acids or their salts, halides or anhydrides
- C07C51/42—Separation; Purification; Stabilisation; Use of additives
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07C—ACYCLIC OR CARBOCYCLIC COMPOUNDS
- C07C65/00—Compounds having carboxyl groups bound to carbon atoms of six—membered aromatic rings and containing any of the groups OH, O—metal, —CHO, keto, ether, groups, groups, or groups
- C07C65/32—Compounds having carboxyl groups bound to carbon atoms of six—membered aromatic rings and containing any of the groups OH, O—metal, —CHO, keto, ether, groups, groups, or groups containing keto groups
- C07C65/40—Compounds having carboxyl groups bound to carbon atoms of six—membered aromatic rings and containing any of the groups OH, O—metal, —CHO, keto, ether, groups, groups, or groups containing keto groups containing singly bound oxygen-containing groups
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12M—APPARATUS FOR ENZYMOLOGY OR MICROBIOLOGY; APPARATUS FOR CULTURING MICROORGANISMS FOR PRODUCING BIOMASS, FOR GROWING CELLS OR FOR OBTAINING FERMENTATION OR METABOLIC PRODUCTS, i.e. BIOREACTORS OR FERMENTERS
- C12M33/00—Means for introduction, transport, positioning, extraction, harvesting, peeling or sampling of biological material in or from the apparatus
-
- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1003—Extracting or separating nucleic acids from biological samples, e.g. pure separation or isolation methods; Conditions, buffers or apparatuses therefor
-
- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1003—Extracting or separating nucleic acids from biological samples, e.g. pure separation or isolation methods; Conditions, buffers or apparatuses therefor
- C12N15/1006—Extracting or separating nucleic acids from biological samples, e.g. pure separation or isolation methods; Conditions, buffers or apparatuses therefor by means of a solid support carrier, e.g. particles, polymers
-
- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1003—Extracting or separating nucleic acids from biological samples, e.g. pure separation or isolation methods; Conditions, buffers or apparatuses therefor
- C12N15/1006—Extracting or separating nucleic acids from biological samples, e.g. pure separation or isolation methods; Conditions, buffers or apparatuses therefor by means of a solid support carrier, e.g. particles, polymers
- C12N15/101—Extracting or separating nucleic acids from biological samples, e.g. pure separation or isolation methods; Conditions, buffers or apparatuses therefor by means of a solid support carrier, e.g. particles, polymers by chromatography, e.g. electrophoresis, ion-exchange, reverse phase
-
- 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
- C12Q1/02—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving viable microorganisms
- C12Q1/04—Determining presence or kind of microorganism; Use of selective media for testing antibiotics or bacteriocides; Compositions containing a chemical indicator therefor
-
- 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
- C12Q1/02—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving viable microorganisms
- C12Q1/24—Methods of sampling, or inoculating or spreading a sample; Methods of physically isolating an intact microorganisms
-
- 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
- C12Q1/56—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving blood clotting factors, e.g. involving thrombin, thromboplastin, fibrinogen
-
- 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
- C12Q1/68—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving nucleic acids
- C12Q1/6806—Preparing nucleic acids for analysis, e.g. for polymerase chain reaction [PCR] assay
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N1/00—Sampling; Preparing specimens for investigation
- G01N1/28—Preparing specimens for investigation including physical details of (bio-)chemical methods covered elsewhere, e.g. G01N33/50, C12Q
- G01N1/34—Purifying; Cleaning
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/86—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving blood coagulating time or factors, or their receptors
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Molecular Biology (AREA)
- Analytical Chemistry (AREA)
- General Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Physics & Mathematics (AREA)
- Microbiology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Immunology (AREA)
- Hematology (AREA)
- Plant Pathology (AREA)
- Crystallography & Structural Chemistry (AREA)
- Pathology (AREA)
- Urology & Nephrology (AREA)
- General Physics & Mathematics (AREA)
- Medicinal Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Cell Biology (AREA)
- Toxicology (AREA)
- Food Science & Technology (AREA)
- Neurosurgery (AREA)
- Sustainable Development (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Apparatus Associated With Microorganisms And Enzymes (AREA)
- Agricultural Chemicals And Associated Chemicals (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| AU2010207760A AU2010207760B2 (en) | 2003-08-15 | 2010-08-05 | Materials and methods for capture of pathogens and removal of aurintricarboxylic acid from a sample |
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US10/604,779 | 2003-08-15 | ||
| US10/604,779 US7998699B2 (en) | 2002-08-15 | 2003-08-15 | Early detection of pathogens in blood |
| US48189204P | 2004-01-14 | 2004-01-14 | |
| US60/481,892 | 2004-01-14 | ||
| PCT/US2004/026606 WO2005021799A2 (en) | 2003-08-15 | 2004-08-16 | Materials and methods for capture of pathogens and removal of aurintricarboxylic acid from a sample |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2010207760A Division AU2010207760B2 (en) | 2003-08-15 | 2010-08-05 | Materials and methods for capture of pathogens and removal of aurintricarboxylic acid from a sample |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| AU2004269340A1 AU2004269340A1 (en) | 2005-03-10 |
| AU2004269340B2 true AU2004269340B2 (en) | 2010-09-16 |
Family
ID=34840999
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2004269340A Ceased AU2004269340B2 (en) | 2003-08-15 | 2004-08-16 | Materials and methods for capture of pathogens and removal of aurintricarboxylic acid from a sample |
| AU2010207760A Ceased AU2010207760B2 (en) | 2003-08-15 | 2010-08-05 | Materials and methods for capture of pathogens and removal of aurintricarboxylic acid from a sample |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2010207760A Ceased AU2010207760B2 (en) | 2003-08-15 | 2010-08-05 | Materials and methods for capture of pathogens and removal of aurintricarboxylic acid from a sample |
Country Status (13)
| Country | Link |
|---|---|
| US (12) | US7416843B2 (enExample) |
| EP (3) | EP1654387B1 (enExample) |
| JP (2) | JP4662932B2 (enExample) |
| AT (2) | ATE510931T1 (enExample) |
| AU (2) | AU2004269340B2 (enExample) |
| DE (1) | DE602004020999D1 (enExample) |
| DK (2) | DK1654387T3 (enExample) |
| ES (1) | ES2325445T3 (enExample) |
| NO (1) | NO20061189L (enExample) |
| PL (2) | PL1654387T3 (enExample) |
| PT (2) | PT1654387E (enExample) |
| SI (1) | SI1654387T1 (enExample) |
| WO (1) | WO2005021799A2 (enExample) |
Families Citing this family (27)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7998699B2 (en) | 2002-08-15 | 2011-08-16 | University Of South Florida | Early detection of pathogens in blood |
| DE602004020999D1 (de) | 2003-08-15 | 2009-06-18 | Univ South Florida | Materialien und verfahren zum einfangen von krankheitserregern und zur abtrennung von aurintricarbonsäure aus einer probe |
| CY1110678T1 (el) * | 2003-08-15 | 2015-06-10 | University Of South Florida | Υλικα και μεθοδοι για την παγιδευση παθογονων και την απομακρυνση του χρυσινοτρικαρβοξυλικου οξεος απο ενα δειγμα |
| WO2007069983A1 (en) | 2005-12-13 | 2007-06-21 | Exthera Ab | Method for extracorporeal removal of a pathogenic microbe, an inflammatory cell or an inflammatory protein from blood |
| CA2576682A1 (en) | 2006-03-08 | 2007-09-08 | Martinrea International Inc. | Electrolyte delivery system |
| EP2137323A4 (en) * | 2007-02-28 | 2011-01-12 | Ge Healthcare Bio Sciences | ROOM TEMPERATURE STABLE CHEMICAL / BIOLOGICAL REAGENTS ON MEMBRANES OR FILTERS |
| EP2509604B1 (en) | 2009-12-01 | 2021-03-17 | ExThera Medical Corporation | Device for removing cytokines from blood with surface immobilized polysaccharides |
| EP2333105A1 (en) * | 2009-12-08 | 2011-06-15 | Koninklijke Philips Electronics N.V. | Selective lysis of cells |
| US20110225809A1 (en) * | 2010-03-17 | 2011-09-22 | Alan Francis Daher | Apparatus for removably attaching an item to a surface |
| PT3067431T (pt) * | 2010-09-15 | 2019-10-29 | Debiopharm Int Sa | Dispositivo incluindo componentes sanguíneos para separação de moléculas ou partículas alvo a partir de amostras |
| WO2012112724A1 (en) | 2011-02-15 | 2012-08-23 | Exthera Medical, Llc | Device and method for removal of blood-borne pathogens, toxins and inflammatory cytokines |
| JP2013055888A (ja) * | 2011-09-07 | 2013-03-28 | Toyobo Co Ltd | 血液培養サンプルからの迅速かつ簡便な細菌検出 |
| DK2861273T3 (da) | 2012-06-13 | 2017-11-27 | Exthera Medical Corp | Anvendelse af heparin og kulhydrater til behandling af cancer. |
| FR3001464B1 (fr) | 2013-01-25 | 2016-02-26 | Biomerieux Sa | Procede d'isolement specifique d'acides nucleiques d'interet |
| FR3002452B1 (fr) * | 2013-02-28 | 2016-02-12 | Dermaconcept Jmc | Composition dermatologique antimicrobienne topique |
| JP6648009B2 (ja) | 2013-06-24 | 2020-02-14 | エクステラ・メディカル・コーポレーション | マンノース被覆基材を含有する血液濾過システム |
| CN105705177B (zh) | 2013-11-08 | 2019-10-22 | 艾克塞拉医疗公司 | 使用吸附介质诊断感染性疾病的方法 |
| DE15782250T1 (de) | 2014-04-24 | 2017-08-10 | Exthera Medical Corporation | Verfahren zur Entfernung von Bakterien aus Blut unter Verwendung einer hohen Durchflussrate |
| AU2015321601B2 (en) | 2014-09-22 | 2020-04-23 | Exthera Medical Corporation | Wearable hemoperfusion device |
| CN104749009B (zh) | 2015-03-30 | 2018-05-04 | 上海云泽生物科技有限公司 | 用于免疫分析的免疫抑制剂药物提取试剂 |
| US10786615B2 (en) | 2016-03-02 | 2020-09-29 | Exthera Medical Corporation | Method for treating drug intoxication |
| US11911551B2 (en) | 2016-03-02 | 2024-02-27 | Exthera Medical Corporation | Method for treating drug intoxication |
| GB2557654A (en) * | 2016-12-14 | 2018-06-27 | Uea Enterprises Ltd | Method for nucleic acid depletion |
| US11168323B2 (en) | 2017-06-01 | 2021-11-09 | Nantomics Llc | DNA stabilization of RNA |
| KR20220009400A (ko) | 2019-05-16 | 2022-01-24 | 엑스테라 메디컬 코퍼레이션 | 내피 글리코칼릭스 구조의 조절 방법 |
| EP4025042A4 (en) * | 2019-09-06 | 2023-06-14 | The Trustees of Indiana University | Novel compositions for disrupting biofilms |
| US20240271184A1 (en) * | 2021-06-08 | 2024-08-15 | Dna Genotek Inc. | Low ph composition and method for stabilizing nucleic acids in biological samples |
Family Cites Families (33)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US1541947A (en) | 1922-03-21 | 1925-06-16 | Electric Water Sterilizer & Oz | Electrolytic cell |
| US3130038A (en) * | 1961-03-13 | 1964-04-21 | Int Minerals & Chem Corp | Granular fertilizers |
| US3245780A (en) | 1961-04-13 | 1966-04-12 | Phillip A Hunt Chemical Corp | Nickel stripping ammoniacal solution containing a nitro benzene compound |
| US3378443A (en) | 1966-04-05 | 1968-04-16 | American Cyanamid Co | Anhydrous liquid suspensions of biologics |
| US4693972A (en) * | 1984-01-16 | 1987-09-15 | Becton, Dickinson And Company | Composition and method for rapid detection of microorganisms in clinical samples |
| US4636524A (en) | 1984-12-06 | 1987-01-13 | Biomatrix, Inc. | Cross-linked gels of hyaluronic acid and products containing such gels |
| US6027877A (en) | 1993-11-04 | 2000-02-22 | Gene Check, Inc. | Use of immobilized mismatch binding protein for detection of mutations and polymorphisms, purification of amplified DNA samples and allele identification |
| US5789462A (en) | 1995-09-13 | 1998-08-04 | Seikagaku Kogyo Kabushiki Kaisha (Seikagaku Corporation) | Photocured crosslinked-hyaluronic acid contact lens |
| US6825047B1 (en) | 1996-04-03 | 2004-11-30 | Applera Corporation | Device and method for multiple analyte detection |
| US5925552A (en) | 1996-04-25 | 1999-07-20 | Medtronic, Inc. | Method for attachment of biomolecules to medical devices surfaces |
| US6103525A (en) | 1996-10-17 | 2000-08-15 | The Regents Of The University Of California | Hybridoma cell lines producing monoclonal antibodies that bind to human plasma hyaluronidase |
| SE9604610D0 (sv) | 1996-12-16 | 1996-12-16 | Noviscens Ab | Medical composition |
| US6368871B1 (en) | 1997-08-13 | 2002-04-09 | Cepheid | Non-planar microstructures for manipulation of fluid samples |
| JP4196236B2 (ja) * | 1998-03-17 | 2008-12-17 | 東洋紡績株式会社 | 核酸増幅用試薬および配列特異的な核酸増幅法 |
| US6091979A (en) | 1998-07-07 | 2000-07-18 | Children's Medical Center Corporation | Subdural electrode arrays for monitoring cortical electrical activity |
| US6592814B2 (en) | 1998-10-02 | 2003-07-15 | Johnson & Johnson Vision Care, Inc. | Biomedical devices with antimicrobial coatings |
| WO2000041732A1 (en) | 1999-01-19 | 2000-07-20 | The Children's Hospital Of Philadelphia | Hydrogel compositions for controlled delivery of virus vectors and methods of use thereof |
| ATE419528T1 (de) | 1999-04-28 | 2009-01-15 | Eidgenoess Tech Hochschule | Polyionische beschichtungen für analytische und sensor-vorrichtungen |
| US7306924B2 (en) | 2000-04-17 | 2007-12-11 | Purdue Research Foundation | Biosensor and related method |
| US6632610B2 (en) | 2000-10-12 | 2003-10-14 | Gensat S.A. | Methods of identification and isolation of polynucleotides containing nucleic acid differences |
| US7001724B1 (en) * | 2000-11-28 | 2006-02-21 | Applera Corporation | Compositions, methods, and kits for isolating nucleic acids using surfactants and proteases |
| US7192445B2 (en) | 2000-12-06 | 2007-03-20 | Astra Tech Ab | Medical prosthetic devices and implants having improved biocompatibility |
| DE10108483A1 (de) | 2001-02-22 | 2002-09-05 | Bayer Ag | Phosphorhaltige Polymere für optischen Signalwandler |
| AU2002258490A1 (en) | 2001-03-12 | 2003-06-17 | Clemson University | Polysaccharide-based polmerizable hydrogels |
| CN100494360C (zh) | 2001-03-22 | 2009-06-03 | 博奥生物有限公司 | 细胞分离方法及其应用 |
| WO2003048295A1 (en) | 2001-11-30 | 2003-06-12 | Fluidigm Corporation | Microfluidic device and methods of using same |
| US7482116B2 (en) | 2002-06-07 | 2009-01-27 | Dna Genotek Inc. | Compositions and methods for obtaining nucleic acids from sputum |
| US7998699B2 (en) | 2002-08-15 | 2011-08-16 | University Of South Florida | Early detection of pathogens in blood |
| US7402279B2 (en) | 2002-10-31 | 2008-07-22 | Agilent Technologies, Inc. | Device with integrated microfluidic and electronic components |
| JP4166587B2 (ja) | 2003-01-24 | 2008-10-15 | 株式会社サキコーポレーション | 外観検査装置および体積検査方法 |
| US7476363B2 (en) | 2003-04-03 | 2009-01-13 | Fluidigm Corporation | Microfluidic devices and methods of using same |
| US7687239B2 (en) | 2003-07-12 | 2010-03-30 | Accelrs Technology Corporation | Sensitive and rapid determination of antimicrobial susceptibility |
| DE602004020999D1 (de) * | 2003-08-15 | 2009-06-18 | Univ South Florida | Materialien und verfahren zum einfangen von krankheitserregern und zur abtrennung von aurintricarbonsäure aus einer probe |
-
2004
- 2004-08-16 DE DE602004020999T patent/DE602004020999D1/de not_active Expired - Lifetime
- 2004-08-16 DK DK04801986T patent/DK1654387T3/da active
- 2004-08-16 PL PL04801986T patent/PL1654387T3/pl unknown
- 2004-08-16 AT AT09159214T patent/ATE510931T1/de active
- 2004-08-16 AT AT04801986T patent/ATE430812T1/de active
- 2004-08-16 AU AU2004269340A patent/AU2004269340B2/en not_active Ceased
- 2004-08-16 ES ES04801986T patent/ES2325445T3/es not_active Expired - Lifetime
- 2004-08-16 EP EP04801986A patent/EP1654387B1/en not_active Expired - Lifetime
- 2004-08-16 WO PCT/US2004/026606 patent/WO2005021799A2/en not_active Ceased
- 2004-08-16 PT PT04801986T patent/PT1654387E/pt unknown
- 2004-08-16 PL PL09159214T patent/PL2103694T3/pl unknown
- 2004-08-16 JP JP2006523971A patent/JP4662932B2/ja not_active Expired - Fee Related
- 2004-08-16 DK DK09159214.7T patent/DK2103694T3/da active
- 2004-08-16 PT PT09159214T patent/PT2103694E/pt unknown
- 2004-08-16 EP EP09165293.3A patent/EP2112232B1/en not_active Expired - Lifetime
- 2004-08-16 SI SI200431179T patent/SI1654387T1/sl unknown
- 2004-08-16 EP EP09159214A patent/EP2103694B1/en not_active Expired - Lifetime
-
2005
- 2005-01-14 US US11/035,667 patent/US7416843B2/en not_active Expired - Lifetime
-
2006
- 2006-03-14 NO NO20061189A patent/NO20061189L/no not_active Application Discontinuation
-
2008
- 2008-05-08 US US12/117,505 patent/US8465966B2/en not_active Expired - Fee Related
-
2010
- 2010-05-11 JP JP2010108850A patent/JP5253451B2/ja not_active Expired - Fee Related
- 2010-08-05 AU AU2010207760A patent/AU2010207760B2/en not_active Ceased
-
2012
- 2012-12-21 US US13/725,651 patent/US20130130302A1/en not_active Abandoned
- 2012-12-21 US US13/725,568 patent/US8927243B2/en not_active Expired - Fee Related
- 2012-12-21 US US13/725,113 patent/US8916698B2/en not_active Expired - Fee Related
- 2012-12-21 US US13/725,303 patent/US8574866B2/en not_active Expired - Fee Related
- 2012-12-21 US US13/725,924 patent/US8815502B2/en not_active Expired - Fee Related
- 2012-12-21 US US13/725,495 patent/US8962243B2/en not_active Expired - Fee Related
- 2012-12-21 US US13/725,196 patent/US8592200B2/en not_active Expired - Fee Related
- 2012-12-21 US US13/725,435 patent/US8759479B2/en not_active Expired - Fee Related
-
2013
- 2013-01-04 US US13/734,367 patent/US8785176B2/en not_active Expired - Fee Related
- 2013-03-28 US US13/852,938 patent/US8735090B2/en not_active Expired - Lifetime
Non-Patent Citations (1)
| Title |
|---|
| Kiss C. et al. Journal of virological Methods, 2003, vol. 107, pp. 195-203 * |
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| AU2010207760B2 (en) | Materials and methods for capture of pathogens and removal of aurintricarboxylic acid from a sample | |
| AU2012216623B2 (en) | Materials and methods for capture of pathogens and removal of aurintricarboxylic acid from a sample | |
| AU2013203143B2 (en) | Materials and methods for capture of pathogens and removal of aurintricarboxylic acid from a sample | |
| JP2013005820A (ja) | 試料からの病原体の捕獲およびアウリントリカルボン酸除去のための物質および方法 | |
| HK1136852B (en) | Methods for extracting pathogen nucleic acid from a blood sample using aurintricarboxylic acid | |
| HK1136317B (en) | Materials and methods for capture of pathogens and removal of aurintricarboxylic acid from a sample |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FGA | Letters patent sealed or granted (standard patent) | ||
| MK14 | Patent ceased section 143(a) (annual fees not paid) or expired |