JPS6027517B2 - その場で重合させて蛋白質を固定化する方法 - Google Patents
その場で重合させて蛋白質を固定化する方法Info
- Publication number
- JPS6027517B2 JPS6027517B2 JP51142369A JP14236976A JPS6027517B2 JP S6027517 B2 JPS6027517 B2 JP S6027517B2 JP 51142369 A JP51142369 A JP 51142369A JP 14236976 A JP14236976 A JP 14236976A JP S6027517 B2 JPS6027517 B2 JP S6027517B2
- Authority
- JP
- Japan
- Prior art keywords
- support
- urease
- protein
- item
- enzyme
- 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
Links
- 238000000034 method Methods 0.000 title claims description 42
- 102000004169 proteins and genes Human genes 0.000 title claims description 37
- 108090000623 proteins and genes Proteins 0.000 title claims description 37
- 230000003100 immobilizing effect Effects 0.000 title claims description 7
- 230000000379 polymerizing effect Effects 0.000 title description 3
- 108010046334 Urease Proteins 0.000 claims description 81
- 102000004190 Enzymes Human genes 0.000 claims description 67
- 108090000790 Enzymes Proteins 0.000 claims description 67
- 235000018102 proteins Nutrition 0.000 claims description 36
- 238000006116 polymerization reaction Methods 0.000 claims description 31
- 239000000843 powder Substances 0.000 claims description 11
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims description 9
- 235000018417 cysteine Nutrition 0.000 claims description 9
- 238000011065 in-situ storage Methods 0.000 claims description 9
- 229960003067 cystine Drugs 0.000 claims description 8
- 239000007864 aqueous solution Substances 0.000 claims description 7
- 238000007596 consolidation process Methods 0.000 claims description 7
- 239000011159 matrix material Substances 0.000 claims description 3
- 239000000835 fiber Substances 0.000 claims description 2
- TWNQGVIAIRXVLR-UHFFFAOYSA-N oxo(oxoalumanyloxy)alumane Chemical compound O=[Al]O[Al]=O TWNQGVIAIRXVLR-UHFFFAOYSA-N 0.000 claims 1
- 238000005245 sintering Methods 0.000 claims 1
- 229940088598 enzyme Drugs 0.000 description 63
- PNEYBMLMFCGWSK-UHFFFAOYSA-N aluminium oxide Inorganic materials [O-2].[O-2].[O-2].[Al+3].[Al+3] PNEYBMLMFCGWSK-UHFFFAOYSA-N 0.000 description 62
- 239000000872 buffer Substances 0.000 description 43
- 239000000243 solution Substances 0.000 description 37
- 239000000203 mixture Substances 0.000 description 30
- POSZUTFLHGNLHX-KSBRXOFISA-N tris maleate Chemical compound OCC(N)(CO)CO.OCC(N)(CO)CO.OC(=O)\C=C/C(O)=O POSZUTFLHGNLHX-KSBRXOFISA-N 0.000 description 22
- 230000000694 effects Effects 0.000 description 18
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 14
- 239000006228 supernatant Substances 0.000 description 13
- 239000002131 composite material Substances 0.000 description 12
- 239000012153 distilled water Substances 0.000 description 12
- 238000004458 analytical method Methods 0.000 description 11
- 230000000977 initiatory effect Effects 0.000 description 11
- 239000002245 particle Substances 0.000 description 10
- 238000006243 chemical reaction Methods 0.000 description 8
- 238000001179 sorption measurement Methods 0.000 description 8
- 239000008351 acetate buffer Substances 0.000 description 7
- 150000001875 compounds Chemical class 0.000 description 7
- 238000003860 storage Methods 0.000 description 7
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
- 239000002253 acid Substances 0.000 description 6
- LEVWYRKDKASIDU-QWWZWVQMSA-N D-cystine Chemical compound OC(=O)[C@H](N)CSSC[C@@H](N)C(O)=O LEVWYRKDKASIDU-QWWZWVQMSA-N 0.000 description 5
- 239000012528 membrane Substances 0.000 description 5
- VLEIUWBSEKKKFX-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;2-[2-[bis(carboxymethyl)amino]ethyl-(carboxymethyl)amino]acetic acid Chemical compound OCC(N)(CO)CO.OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O VLEIUWBSEKKKFX-UHFFFAOYSA-N 0.000 description 4
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 4
- 125000000539 amino acid group Chemical group 0.000 description 4
- -1 cysteine amino acids Chemical class 0.000 description 4
- 239000008363 phosphate buffer Substances 0.000 description 4
- 229920000642 polymer Polymers 0.000 description 4
- 239000011148 porous material Substances 0.000 description 4
- 102000007698 Alcohol dehydrogenase Human genes 0.000 description 3
- 108010021809 Alcohol dehydrogenase Proteins 0.000 description 3
- 101710088194 Dehydrogenase Proteins 0.000 description 3
- 108010093096 Immobilized Enzymes Proteins 0.000 description 3
- 108010008292 L-Amino Acid Oxidase Proteins 0.000 description 3
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 239000007983 Tris buffer Substances 0.000 description 3
- 150000007513 acids Chemical class 0.000 description 3
- 235000001014 amino acid Nutrition 0.000 description 3
- 238000006555 catalytic reaction Methods 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 230000007774 longterm Effects 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 238000012545 processing Methods 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 239000011541 reaction mixture Substances 0.000 description 3
- 230000008707 rearrangement Effects 0.000 description 3
- 238000011160 research Methods 0.000 description 3
- 239000001632 sodium acetate Substances 0.000 description 3
- 235000017281 sodium acetate Nutrition 0.000 description 3
- BHZOKUMUHVTPBX-UHFFFAOYSA-M sodium acetic acid acetate Chemical compound [Na+].CC(O)=O.CC([O-])=O BHZOKUMUHVTPBX-UHFFFAOYSA-M 0.000 description 3
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 3
- 238000000108 ultra-filtration Methods 0.000 description 3
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 2
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 2
- 102000030789 Histidine Ammonia-Lyase Human genes 0.000 description 2
- 108700006308 Histidine ammonia-lyases Proteins 0.000 description 2
- 102000007070 L-amino-acid oxidase Human genes 0.000 description 2
- CPLXHLVBOLITMK-UHFFFAOYSA-N Magnesium oxide Chemical compound [Mg]=O CPLXHLVBOLITMK-UHFFFAOYSA-N 0.000 description 2
- 229910019142 PO4 Inorganic materials 0.000 description 2
- 229910000831 Steel Inorganic materials 0.000 description 2
- MCMNRKCIXSYSNV-UHFFFAOYSA-N Zirconium dioxide Chemical compound O=[Zr]=O MCMNRKCIXSYSNV-UHFFFAOYSA-N 0.000 description 2
- 150000001413 amino acids Chemical class 0.000 description 2
- 230000001588 bifunctional effect Effects 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 239000007853 buffer solution Substances 0.000 description 2
- 239000004202 carbamide Substances 0.000 description 2
- 230000002860 competitive effect Effects 0.000 description 2
- 239000012141 concentrate Substances 0.000 description 2
- 230000001627 detrimental effect Effects 0.000 description 2
- XPPKVPWEQAFLFU-UHFFFAOYSA-J diphosphate(4-) Chemical compound [O-]P([O-])(=O)OP([O-])([O-])=O XPPKVPWEQAFLFU-UHFFFAOYSA-J 0.000 description 2
- 235000011180 diphosphates Nutrition 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- 238000010438 heat treatment Methods 0.000 description 2
- 210000003127 knee Anatomy 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 229910052751 metal Inorganic materials 0.000 description 2
- 239000002184 metal Substances 0.000 description 2
- 238000002156 mixing Methods 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 238000007873 sieving Methods 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 239000010959 steel Substances 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 229920002994 synthetic fiber Polymers 0.000 description 2
- 239000012209 synthetic fiber Substances 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 125000003396 thiol group Chemical group [H]S* 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- LXJXRIRHZLFYRP-VKHMYHEASA-L (R)-2-Hydroxy-3-(phosphonooxy)-propanal Natural products O=C[C@H](O)COP([O-])([O-])=O LXJXRIRHZLFYRP-VKHMYHEASA-L 0.000 description 1
- OXRSCXFOUBLJAR-ODZAUARKSA-N (z)-but-2-enedioic acid;methanamine Chemical compound NC.OC(=O)\C=C/C(O)=O OXRSCXFOUBLJAR-ODZAUARKSA-N 0.000 description 1
- BDDLHHRCDSJVKV-UHFFFAOYSA-N 7028-40-2 Chemical compound CC(O)=O.CC(O)=O.CC(O)=O.CC(O)=O BDDLHHRCDSJVKV-UHFFFAOYSA-N 0.000 description 1
- 229920002972 Acrylic fiber Polymers 0.000 description 1
- 101000808346 Canavalia ensiformis Urease Proteins 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 1
- 229920000742 Cotton Polymers 0.000 description 1
- 239000004971 Cross linker Substances 0.000 description 1
- LXJXRIRHZLFYRP-VKHMYHEASA-N D-glyceraldehyde 3-phosphate Chemical compound O=C[C@H](O)COP(O)(O)=O LXJXRIRHZLFYRP-VKHMYHEASA-N 0.000 description 1
- 101100080807 Drosophila melanogaster mt:ND2 gene Proteins 0.000 description 1
- PIICEJLVQHRZGT-UHFFFAOYSA-N Ethylenediamine Chemical compound NCCN PIICEJLVQHRZGT-UHFFFAOYSA-N 0.000 description 1
- 102000016901 Glutamate dehydrogenase Human genes 0.000 description 1
- 108700023156 Glutamate dehydrogenases Proteins 0.000 description 1
- 108010036164 Glutathione synthase Proteins 0.000 description 1
- 102100034294 Glutathione synthetase Human genes 0.000 description 1
- 108010088390 Glycine N-Methyltransferase Proteins 0.000 description 1
- 102000008764 Glycine N-methyltransferase Human genes 0.000 description 1
- 108010001483 Glycogen Synthase Proteins 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 102000014702 Haptoglobin Human genes 0.000 description 1
- 108050005077 Haptoglobin Proteins 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 102100026388 L-amino-acid oxidase Human genes 0.000 description 1
- 101150016680 MT-ND2 gene Proteins 0.000 description 1
- LSDPWZHWYPCBBB-UHFFFAOYSA-N Methanethiol Chemical compound SC LSDPWZHWYPCBBB-UHFFFAOYSA-N 0.000 description 1
- 102100028488 NADH-ubiquinone oxidoreductase chain 2 Human genes 0.000 description 1
- 101150102231 ND2 gene Proteins 0.000 description 1
- 239000004677 Nylon Substances 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 239000004698 Polyethylene Substances 0.000 description 1
- 239000004743 Polypropylene Substances 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 241000589540 Pseudomonas fluorescens Species 0.000 description 1
- 229920000297 Rayon Polymers 0.000 description 1
- 240000003243 Thuja occidentalis Species 0.000 description 1
- 235000008109 Thuja occidentalis Nutrition 0.000 description 1
- YKTSYUJCYHOUJP-UHFFFAOYSA-N [O--].[Al+3].[Al+3].[O-][Si]([O-])([O-])[O-] Chemical compound [O--].[Al+3].[Al+3].[O-][Si]([O-])([O-])[O-] YKTSYUJCYHOUJP-UHFFFAOYSA-N 0.000 description 1
- NABCNSQIAUKDCR-UHFFFAOYSA-N [[4-(4-diazonioimino-2-sulfocyclohexa-2,5-dien-1-ylidene)-3-sulfocyclohexa-2,5-dien-1-ylidene]hydrazinylidene]azanide Chemical compound OS(=O)(=O)C1=CC(N=[N+]=[N-])=CC=C1C1=CC=C(N=[N+]=[N-])C=C1S(O)(=O)=O NABCNSQIAUKDCR-UHFFFAOYSA-N 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 238000010420 art technique Methods 0.000 description 1
- 239000010425 asbestos Substances 0.000 description 1
- 239000003899 bactericide agent Substances 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 230000003139 buffering effect Effects 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 239000000919 ceramic Substances 0.000 description 1
- 229910010293 ceramic material Inorganic materials 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 239000004927 clay Substances 0.000 description 1
- 238000005056 compaction Methods 0.000 description 1
- 238000009833 condensation Methods 0.000 description 1
- 230000005494 condensation Effects 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 239000010949 copper Substances 0.000 description 1
- 239000007822 coupling agent Substances 0.000 description 1
- 239000003431 cross linking reagent Substances 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- LEVWYRKDKASIDU-IMJSIDKUSA-N cystine group Chemical group C([C@@H](C(=O)O)N)SSC[C@@H](C(=O)O)N LEVWYRKDKASIDU-IMJSIDKUSA-N 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 238000003795 desorption Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 125000002228 disulfide group Chemical group 0.000 description 1
- 150000002019 disulfides Chemical class 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 239000002657 fibrous material Substances 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 238000001641 gel filtration chromatography Methods 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- AWUCVROLDVIAJX-UHFFFAOYSA-N glycerol 1-phosphate Chemical compound OCC(O)COP(O)(O)=O AWUCVROLDVIAJX-UHFFFAOYSA-N 0.000 description 1
- 108010083391 glycinin Proteins 0.000 description 1
- 150000004820 halides Chemical class 0.000 description 1
- 108060003552 hemocyanin Proteins 0.000 description 1
- 125000004029 hydroxymethyl group Chemical group [H]OC([H])([H])* 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 239000012784 inorganic fiber Substances 0.000 description 1
- 238000004811 liquid chromatography Methods 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 239000000395 magnesium oxide Substances 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 150000002739 metals Chemical class 0.000 description 1
- FTQWRYSLUYAIRQ-UHFFFAOYSA-N n-[(octadecanoylamino)methyl]octadecanamide Chemical class CCCCCCCCCCCCCCCCCC(=O)NCNC(=O)CCCCCCCCCCCCCCCCC FTQWRYSLUYAIRQ-UHFFFAOYSA-N 0.000 description 1
- BOPGDPNILDQYTO-NNYOXOHSSA-N nicotinamide-adenine dinucleotide Chemical compound C1=CCC(C(=O)N)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 BOPGDPNILDQYTO-NNYOXOHSSA-N 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
- 229920000620 organic polymer Polymers 0.000 description 1
- 229910052574 oxide ceramic Inorganic materials 0.000 description 1
- 239000011224 oxide ceramic Substances 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 239000012466 permeate Substances 0.000 description 1
- 229920000728 polyester Polymers 0.000 description 1
- 229920000573 polyethylene Polymers 0.000 description 1
- 229920001228 polyisocyanate Polymers 0.000 description 1
- 239000005056 polyisocyanate Substances 0.000 description 1
- 229920001155 polypropylene Polymers 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 230000002028 premature Effects 0.000 description 1
- 239000010453 quartz Substances 0.000 description 1
- 239000002964 rayon Substances 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 239000011214 refractory ceramic Substances 0.000 description 1
- 238000005057 refrigeration Methods 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 229910052895 riebeckite Inorganic materials 0.000 description 1
- 239000004576 sand Substances 0.000 description 1
- 239000000377 silicon dioxide Substances 0.000 description 1
- 229910052709 silver Inorganic materials 0.000 description 1
- 239000004332 silver Substances 0.000 description 1
- 238000002791 soaking Methods 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- HLWRUJAIJJEZDL-UHFFFAOYSA-M sodium;2-[2-[bis(carboxymethyl)amino]ethyl-(carboxymethyl)amino]acetate Chemical compound [Na+].OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC([O-])=O HLWRUJAIJJEZDL-UHFFFAOYSA-M 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000002798 spectrophotometry method Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- FRGKKTITADJNOE-UHFFFAOYSA-N sulfanyloxyethane Chemical compound CCOS FRGKKTITADJNOE-UHFFFAOYSA-N 0.000 description 1
- 239000000454 talc Substances 0.000 description 1
- 229910052623 talc Inorganic materials 0.000 description 1
- ZCUFMDLYAMJYST-UHFFFAOYSA-N thorium dioxide Chemical compound O=[Th]=O ZCUFMDLYAMJYST-UHFFFAOYSA-N 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 238000003828 vacuum filtration Methods 0.000 description 1
- 239000011534 wash buffer Substances 0.000 description 1
- 210000002268 wool Anatomy 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
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/14—Enzymes or microbial cells immobilised on or in an inorganic carrier
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/81—Carrier - bound or immobilized peptides or proteins and the preparation thereof, e.g. biological cell or cell fragment as carrier
- Y10S530/811—Peptides or proteins is immobilized on, or in, an inorganic carrier
Landscapes
- Chemical & Material Sciences (AREA)
- Genetics & Genomics (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Organic Chemistry (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Biomedical Technology (AREA)
- Inorganic Chemistry (AREA)
- Biotechnology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Microbiology (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
- Enzymes And Modification Thereof (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US05/666,819 US4008126A (en) | 1976-03-15 | 1976-03-15 | Immobilization of proteins by in-situ polymerization |
| US666819 | 1976-03-15 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS52110890A JPS52110890A (en) | 1977-09-17 |
| JPS6027517B2 true JPS6027517B2 (ja) | 1985-06-29 |
Family
ID=24675628
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP51142369A Expired JPS6027517B2 (ja) | 1976-03-15 | 1976-11-29 | その場で重合させて蛋白質を固定化する方法 |
Country Status (8)
| Country | Link |
|---|---|
| US (1) | US4008126A (enExample) |
| JP (1) | JPS6027517B2 (enExample) |
| AU (1) | AU505623B2 (enExample) |
| CA (1) | CA1067434A (enExample) |
| DE (1) | DE2707024C2 (enExample) |
| FR (1) | FR2344566A1 (enExample) |
| GB (1) | GB1534412A (enExample) |
| NL (1) | NL7613684A (enExample) |
Families Citing this family (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE2732301C3 (de) * | 1977-07-16 | 1980-12-11 | Roehm Gmbh, 6100 Darmstadt | Verfahren zur Herstellung von stabilisierten trägergebundenen Proteinen |
| US4204040A (en) * | 1977-11-18 | 1980-05-20 | Technicon Instruments Corporation | Copolymerization of proteins on an inorganic support |
| US4176006A (en) * | 1978-01-13 | 1979-11-27 | Redpath Sugars Limited | Enzyme immobilization with a disulphide bridge |
| ZA811104B (en) * | 1980-02-26 | 1982-03-31 | Tate & Lyle Ltd | Immobilized enzymes, a process for their preparation and their use in converting substrates to products |
| US4716116A (en) * | 1980-12-04 | 1987-12-29 | Owens-Illinois Glass Container Inc. | Protein modification to provide enzyme activity |
| US4748121A (en) * | 1984-11-30 | 1988-05-31 | Ppg Industries, Inc. | Porous glass fibers with immobilized biochemically active material |
| IL77419A (en) * | 1984-12-21 | 1989-03-31 | Sleytr Uwe B | Production of structures having membranes with continuous pores,method of altering the effective pore size of such structures and the use of structures thus produced or altered |
| SE455103B (sv) * | 1985-01-09 | 1988-06-20 | Lars Edgar Martin Ehrnford | Berare for immobilisering av biologiskt aktivt organiskt material, vilken utgores av sammanfogade partiklar av en poros sintrad glasfibermatris |
| JPH0732B2 (ja) * | 1985-02-26 | 1995-01-11 | 富士デヴイソン化学株式会社 | 細胞培養担体及び細胞培養方法 |
| US6927051B1 (en) | 2002-04-04 | 2005-08-09 | The University Of Akron | Polymer-protein surfactants |
| US7723084B2 (en) * | 2002-06-18 | 2010-05-25 | The University Of Akron | Fibrous protein-immobilization systems |
| WO2011153464A2 (en) * | 2010-06-03 | 2011-12-08 | New York University | In situ oriented immobilization of proteins on a support |
-
1976
- 1976-03-15 US US05/666,819 patent/US4008126A/en not_active Expired - Lifetime
- 1976-10-28 CA CA264,410A patent/CA1067434A/en not_active Expired
- 1976-11-02 GB GB45442/76A patent/GB1534412A/en not_active Expired
- 1976-11-08 AU AU19389/76A patent/AU505623B2/en not_active Expired
- 1976-11-22 FR FR7635111A patent/FR2344566A1/fr active Granted
- 1976-11-29 JP JP51142369A patent/JPS6027517B2/ja not_active Expired
- 1976-12-09 NL NL7613684A patent/NL7613684A/xx not_active Application Discontinuation
-
1977
- 1977-02-18 DE DE2707024A patent/DE2707024C2/de not_active Expired
Also Published As
| Publication number | Publication date |
|---|---|
| JPS52110890A (en) | 1977-09-17 |
| CA1067434A (en) | 1979-12-04 |
| AU505623B2 (en) | 1979-11-29 |
| DE2707024A1 (de) | 1977-09-22 |
| DE2707024C2 (de) | 1982-05-13 |
| FR2344566B1 (enExample) | 1980-03-07 |
| AU1938976A (en) | 1978-05-18 |
| US4008126A (en) | 1977-02-15 |
| FR2344566A1 (fr) | 1977-10-14 |
| NL7613684A (nl) | 1977-09-19 |
| GB1534412A (en) | 1978-12-06 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US6852818B1 (en) | Molecularly imprinted polymers produced by template polymerization | |
| JPS6027517B2 (ja) | その場で重合させて蛋白質を固定化する方法 | |
| US5976527A (en) | High surface area support having bound latex particles containing oxirane groups for immobilization of substances | |
| JPS6029474B2 (ja) | 固定された蛋白質及びその製造法 | |
| EP0154315B1 (en) | Improved diazonium affinity matrixes | |
| EP0423938B1 (en) | Ligand-containing medium for chromatographic separation, process for preparing the medium, and use of the medium for isolating synthetic or natural molecules from a fluid mixture | |
| JPS6356501A (ja) | アフイニテイークロマトグラフイー用カラム充填剤及びその製造方法 | |
| EP1137669B1 (en) | Storage-stable composition comprising squaric acid activated carrier usable for immobilisation of compounds containing amine groups | |
| JP3441530B2 (ja) | 温度応答型分離材料及びその製造方法 | |
| JP3441496B2 (ja) | アフィニティー分離材料 | |
| JPH0489500A (ja) | アフィニティクロマトグラフィーによる物質の精製法および精製装置 | |
| US6524482B2 (en) | Use of ion binding ligands attached to solid supports and membranes for ion removal from a biological system | |
| Yavuz et al. | Dye affinity hollow fibers for albumin purification | |
| Yavuz et al. | Cibacron Blue F3GA incorporated poly (methylmethacrylate) beads for albumin adsorption in batch system | |
| CN110437491B (zh) | 纳豆激酶表面分子印迹聚合物及其制备方法和应用 | |
| EP0596315B1 (en) | A method of attaching dialdehyde starch to a surface and products produced by that method | |
| US5395856A (en) | HPLC avidin monomer affinity resin | |
| US4204040A (en) | Copolymerization of proteins on an inorganic support | |
| Yavuz et al. | Molecular recognition based iron removal from human plasma with imprinted membranes | |
| JPS63304000A (ja) | 生体由来物質の固定化方法 | |
| WO1994017903B1 (en) | Membranes for use in affinity separation and methods for activating membranes | |
| JPH0796617B2 (ja) | 塩化スルフリル−ポリアミド誘導体 | |
| Leonovich et al. | Biocompatible Molecularly Imprinted Cryogel Matrices for Protein Recognition in Biological Samples | |
| KR100516824B1 (ko) | 불포화지방산을 이용한 생체분자 고정용 고체 지지체의 제조방법, 이에 의해 제조된 고체 지지체, 및 이를 이용한 효소 고정화 방법 | |
| Ayhan et al. | Protein A immobilized poly (methylmethacrylate-co-hydroxyethylmethacrylate) microbeads for IgG adsorption |