CA2062941A1 - Procede pour lyophiliser les cellules, matieres et plaquettes de type cellules dans un melange de polymeres amphipatiques biocompatibles - Google Patents
Procede pour lyophiliser les cellules, matieres et plaquettes de type cellules dans un melange de polymeres amphipatiques biocompatiblesInfo
- Publication number
- CA2062941A1 CA2062941A1 CA002062941A CA2062941A CA2062941A1 CA 2062941 A1 CA2062941 A1 CA 2062941A1 CA 002062941 A CA002062941 A CA 002062941A CA 2062941 A CA2062941 A CA 2062941A CA 2062941 A1 CA2062941 A1 CA 2062941A1
- Authority
- CA
- Canada
- Prior art keywords
- cells
- medium according
- medium
- molecular weight
- red 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.)
- Abandoned
Links
- 238000000034 method Methods 0.000 title claims abstract description 107
- 230000008569 process Effects 0.000 title claims abstract description 82
- 229920000642 polymer Polymers 0.000 title claims abstract description 57
- 239000000203 mixture Substances 0.000 title claims abstract description 36
- 239000000463 material Substances 0.000 title claims description 10
- 238000004108 freeze drying Methods 0.000 claims abstract description 39
- -1 monosaccharide hexoses Chemical class 0.000 claims abstract description 6
- 150000002972 pentoses Chemical class 0.000 claims abstract 6
- 210000004027 cell Anatomy 0.000 claims description 142
- 210000003743 erythrocyte Anatomy 0.000 claims description 91
- 108010054147 Hemoglobins Proteins 0.000 claims description 42
- 102000001554 Hemoglobins Human genes 0.000 claims description 42
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 claims description 39
- 210000004369 blood Anatomy 0.000 claims description 35
- 239000008280 blood Substances 0.000 claims description 35
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 32
- 229920000036 polyvinylpyrrolidone Polymers 0.000 claims description 30
- 239000001267 polyvinylpyrrolidone Substances 0.000 claims description 30
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 claims description 30
- 239000000243 solution Substances 0.000 claims description 24
- 102000004190 Enzymes Human genes 0.000 claims description 22
- 108090000790 Enzymes Proteins 0.000 claims description 22
- 230000000694 effects Effects 0.000 claims description 22
- GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 claims description 19
- 229920001612 Hydroxyethyl starch Polymers 0.000 claims description 19
- 229940050526 hydroxyethylstarch Drugs 0.000 claims description 19
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 claims description 18
- 229960003180 glutathione Drugs 0.000 claims description 18
- 239000011780 sodium chloride Substances 0.000 claims description 18
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 claims description 15
- 229910000397 disodium phosphate Inorganic materials 0.000 claims description 15
- 102000004169 proteins and genes Human genes 0.000 claims description 15
- 108090000623 proteins and genes Proteins 0.000 claims description 15
- 229960000643 adenine Drugs 0.000 claims description 14
- 239000003963 antioxidant agent Substances 0.000 claims description 14
- 235000006708 antioxidants Nutrition 0.000 claims description 14
- 239000000543 intermediate Substances 0.000 claims description 14
- 150000002772 monosaccharides Chemical class 0.000 claims description 14
- 229930024421 Adenine Natural products 0.000 claims description 13
- 239000008103 glucose Substances 0.000 claims description 13
- 230000003078 antioxidant effect Effects 0.000 claims description 12
- 239000002738 chelating agent Substances 0.000 claims description 12
- GVJHHUAWPYXKBD-IEOSBIPESA-N α-tocopherol Chemical compound OC1=C(C)C(C)=C2O[C@@](CCC[C@H](C)CCC[C@H](C)CCCC(C)C)(C)CCC2=C1C GVJHHUAWPYXKBD-IEOSBIPESA-N 0.000 claims description 12
- SRBFZHDQGSBBOR-IOVATXLUSA-N D-xylopyranose Chemical compound O[C@@H]1COC(O)[C@H](O)[C@H]1O SRBFZHDQGSBBOR-IOVATXLUSA-N 0.000 claims description 10
- 108010061951 Methemoglobin Proteins 0.000 claims description 10
- PVNIIMVLHYAWGP-UHFFFAOYSA-N Niacin Chemical compound OC(=O)C1=CC=CN=C1 PVNIIMVLHYAWGP-UHFFFAOYSA-N 0.000 claims description 10
- 210000001772 blood platelet Anatomy 0.000 claims description 9
- 230000002414 glycolytic effect Effects 0.000 claims description 9
- 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 8
- 102000013009 Pyruvate Kinase Human genes 0.000 claims description 8
- 108020005115 Pyruvate Kinase Proteins 0.000 claims description 8
- 210000000170 cell membrane Anatomy 0.000 claims description 8
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 claims description 8
- 235000019800 disodium phosphate Nutrition 0.000 claims description 8
- 239000000126 substance Substances 0.000 claims description 8
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 8
- 108010029692 Bisphosphoglycerate mutase Proteins 0.000 claims description 7
- 108010024636 Glutathione Proteins 0.000 claims description 7
- 102000005548 Hexokinase Human genes 0.000 claims description 7
- 108700040460 Hexokinases Proteins 0.000 claims description 7
- 229930010555 Inosine Natural products 0.000 claims description 7
- UGQMRVRMYYASKQ-KQYNXXCUSA-N Inosine Chemical compound O[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1N1C2=NC=NC(O)=C2N=C1 UGQMRVRMYYASKQ-KQYNXXCUSA-N 0.000 claims description 7
- 210000000601 blood cell Anatomy 0.000 claims description 7
- 229960003786 inosine Drugs 0.000 claims description 7
- 229910000402 monopotassium phosphate Inorganic materials 0.000 claims description 7
- 238000005406 washing Methods 0.000 claims description 7
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 claims description 6
- UBQYURCVBFRUQT-UHFFFAOYSA-N N-benzoyl-Ferrioxamine B Chemical compound CC(=O)N(O)CCCCCNC(=O)CCC(=O)N(O)CCCCCNC(=O)CCC(=O)N(O)CCCCCN UBQYURCVBFRUQT-UHFFFAOYSA-N 0.000 claims description 6
- 229910019142 PO4 Inorganic materials 0.000 claims description 6
- 229940087168 alpha tocopherol Drugs 0.000 claims description 6
- RNBGYGVWRKECFJ-ZXXMMSQZSA-N alpha-D-fructofuranose 1,6-bisphosphate Chemical compound O[C@H]1[C@H](O)[C@](O)(COP(O)(O)=O)O[C@@H]1COP(O)(O)=O RNBGYGVWRKECFJ-ZXXMMSQZSA-N 0.000 claims description 6
- 229960000958 deferoxamine Drugs 0.000 claims description 6
- 238000007710 freezing Methods 0.000 claims description 6
- 230000008014 freezing Effects 0.000 claims description 6
- 229940025237 fructose 1,6-diphosphate Drugs 0.000 claims description 6
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 claims description 6
- 230000003204 osmotic effect Effects 0.000 claims description 6
- 239000010452 phosphate Substances 0.000 claims description 6
- 239000001103 potassium chloride Substances 0.000 claims description 6
- 229960000984 tocofersolan Drugs 0.000 claims description 6
- 239000002076 α-tocopherol Substances 0.000 claims description 6
- 235000004835 α-tocopherol Nutrition 0.000 claims description 6
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 claims description 5
- HMFHBZSHGGEWLO-SOOFDHNKSA-N D-ribofuranose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H]1O HMFHBZSHGGEWLO-SOOFDHNKSA-N 0.000 claims description 5
- 229930091371 Fructose Natural products 0.000 claims description 5
- RFSUNEUAIZKAJO-ARQDHWQXSA-N Fructose Chemical compound OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O RFSUNEUAIZKAJO-ARQDHWQXSA-N 0.000 claims description 5
- 239000005715 Fructose Substances 0.000 claims description 5
- 108010063907 Glutathione Reductase Proteins 0.000 claims description 5
- 102000001105 Phosphofructokinases Human genes 0.000 claims description 5
- 108010069341 Phosphofructokinases Proteins 0.000 claims description 5
- PYMYPHUHKUWMLA-LMVFSUKVSA-N Ribose Natural products OC[C@@H](O)[C@@H](O)[C@@H](O)C=O PYMYPHUHKUWMLA-LMVFSUKVSA-N 0.000 claims description 5
- HMFHBZSHGGEWLO-UHFFFAOYSA-N alpha-D-Furanose-Ribose Natural products OCC1OC(O)C(O)C1O HMFHBZSHGGEWLO-UHFFFAOYSA-N 0.000 claims description 5
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 claims description 5
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 claims description 5
- 238000001035 drying Methods 0.000 claims description 5
- 230000034659 glycolysis Effects 0.000 claims description 5
- 150000002402 hexoses Chemical class 0.000 claims description 5
- 235000001968 nicotinic acid Nutrition 0.000 claims description 5
- 239000011664 nicotinic acid Substances 0.000 claims description 5
- 229960003512 nicotinic acid Drugs 0.000 claims description 5
- XOHUEYCVLUUEJJ-UHFFFAOYSA-N 2,3-Bisphosphoglyceric acid Chemical compound OP(=O)(O)OC(C(=O)O)COP(O)(O)=O XOHUEYCVLUUEJJ-UHFFFAOYSA-N 0.000 claims description 4
- 102100031126 6-phosphogluconolactonase Human genes 0.000 claims description 4
- 108010029731 6-phosphogluconolactonase Proteins 0.000 claims description 4
- 108010018962 Glucosephosphate Dehydrogenase Proteins 0.000 claims description 4
- 102100036442 Glutathione reductase, mitochondrial Human genes 0.000 claims description 4
- 239000007836 KH2PO4 Substances 0.000 claims description 4
- 108020004530 Transaldolase Proteins 0.000 claims description 4
- 102100028601 Transaldolase Human genes 0.000 claims description 4
- 235000019796 monopotassium phosphate Nutrition 0.000 claims description 4
- GNSKLFRGEWLPPA-UHFFFAOYSA-M potassium dihydrogen phosphate Chemical compound [K+].OP(O)([O-])=O GNSKLFRGEWLPPA-UHFFFAOYSA-M 0.000 claims description 4
- 230000008439 repair process Effects 0.000 claims description 4
- LCTONWCANYUPML-UHFFFAOYSA-M Pyruvate Chemical compound CC(=O)C([O-])=O LCTONWCANYUPML-UHFFFAOYSA-M 0.000 claims description 3
- 102000014701 Transketolase Human genes 0.000 claims description 3
- 108010043652 Transketolase Proteins 0.000 claims description 3
- 239000002502 liposome Substances 0.000 claims description 3
- 229910001629 magnesium chloride Inorganic materials 0.000 claims description 3
- 210000004962 mammalian cell Anatomy 0.000 claims description 3
- 230000037361 pathway Effects 0.000 claims description 3
- FQENQNTWSFEDLI-UHFFFAOYSA-J sodium diphosphate Chemical compound [Na+].[Na+].[Na+].[Na+].[O-]P([O-])(=O)OP([O-])([O-])=O FQENQNTWSFEDLI-UHFFFAOYSA-J 0.000 claims description 3
- 229940048086 sodium pyrophosphate Drugs 0.000 claims description 3
- 210000000130 stem cell Anatomy 0.000 claims description 3
- 238000000859 sublimation Methods 0.000 claims description 3
- 230000008022 sublimation Effects 0.000 claims description 3
- 235000019818 tetrasodium diphosphate Nutrition 0.000 claims description 3
- 239000001577 tetrasodium phosphonato phosphate Substances 0.000 claims description 3
- XOHUEYCVLUUEJJ-UHFFFAOYSA-I 2,3-Diphosphoglycerate Chemical compound [O-]P(=O)([O-])OC(C(=O)[O-])COP([O-])([O-])=O XOHUEYCVLUUEJJ-UHFFFAOYSA-I 0.000 claims description 2
- 102000004567 6-phosphogluconate dehydrogenase Human genes 0.000 claims description 2
- 108020001657 6-phosphogluconate dehydrogenase Proteins 0.000 claims description 2
- 101100268493 Cunninghamella elegans 6-PGD gene Proteins 0.000 claims description 2
- VFRROHXSMXFLSN-KCDKBNATSA-N aldehydo-D-galactose 6-phosphate Chemical compound OP(=O)(O)OC[C@@H](O)[C@H](O)[C@H](O)[C@@H](O)C=O VFRROHXSMXFLSN-KCDKBNATSA-N 0.000 claims description 2
- 210000004408 hybridoma Anatomy 0.000 claims description 2
- 210000004976 peripheral blood cell Anatomy 0.000 claims description 2
- 239000008366 buffered solution Substances 0.000 claims 8
- 230000001766 physiological effect Effects 0.000 claims 8
- WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 claims 5
- 108091003079 Bovine Serum Albumin Proteins 0.000 claims 4
- 108091006905 Human Serum Albumin Proteins 0.000 claims 4
- 102000008100 Human Serum Albumin Human genes 0.000 claims 4
- 229940098773 bovine serum albumin Drugs 0.000 claims 4
- ZKHQWZAMYRWXGA-KQYNXXCUSA-N Adenosine triphosphate Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1O ZKHQWZAMYRWXGA-KQYNXXCUSA-N 0.000 claims 2
- 210000004748 cultured cell Anatomy 0.000 claims 2
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 claims 1
- 229960002743 glutamine Drugs 0.000 claims 1
- 238000000338 in vitro Methods 0.000 claims 1
- 235000011164 potassium chloride Nutrition 0.000 claims 1
- 238000002360 preparation method Methods 0.000 claims 1
- 239000000872 buffer Substances 0.000 description 47
- 239000000523 sample Substances 0.000 description 15
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 14
- 239000008188 pellet Substances 0.000 description 13
- 238000003860 storage Methods 0.000 description 13
- 102000009027 Albumins Human genes 0.000 description 9
- 108010088751 Albumins Proteins 0.000 description 9
- 239000013589 supplement Substances 0.000 description 9
- 239000012528 membrane Substances 0.000 description 8
- 239000011534 wash buffer Substances 0.000 description 8
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 6
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 6
- 230000006378 damage Effects 0.000 description 6
- 229910052760 oxygen Inorganic materials 0.000 description 6
- 239000001301 oxygen Substances 0.000 description 6
- 229920002959 polymer blend Polymers 0.000 description 6
- 239000006228 supernatant Substances 0.000 description 6
- 230000004071 biological effect Effects 0.000 description 5
- 150000001720 carbohydrates Chemical class 0.000 description 5
- 235000014633 carbohydrates Nutrition 0.000 description 5
- 238000006243 chemical reaction Methods 0.000 description 5
- 239000003085 diluting agent Substances 0.000 description 5
- 238000005534 hematocrit Methods 0.000 description 5
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 4
- 108010064719 Oxyhemoglobins Proteins 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 239000000306 component Substances 0.000 description 4
- 239000008121 dextrose Substances 0.000 description 4
- 238000004321 preservation Methods 0.000 description 4
- VWDWKYIASSYTQR-UHFFFAOYSA-N sodium nitrate Chemical compound [Na+].[O-][N+]([O-])=O VWDWKYIASSYTQR-UHFFFAOYSA-N 0.000 description 4
- 238000003556 assay Methods 0.000 description 3
- 230000001413 cellular effect Effects 0.000 description 3
- 210000004292 cytoskeleton Anatomy 0.000 description 3
- 230000006872 improvement Effects 0.000 description 3
- 229910052742 iron Inorganic materials 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 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 3
- 239000002953 phosphate buffered saline Substances 0.000 description 3
- 238000011084 recovery Methods 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 2
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 2
- NBSCHQHZLSJFNQ-GASJEMHNSA-N D-Glucose 6-phosphate Chemical compound OC1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H](O)[C@H]1O NBSCHQHZLSJFNQ-GASJEMHNSA-N 0.000 description 2
- KTVPXOYAKDPRHY-SOOFDHNKSA-N D-ribofuranose 5-phosphate Chemical compound OC1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]1O KTVPXOYAKDPRHY-SOOFDHNKSA-N 0.000 description 2
- VFRROHXSMXFLSN-UHFFFAOYSA-N Glc6P Natural products OP(=O)(O)OCC(O)C(O)C(O)C(O)C=O VFRROHXSMXFLSN-UHFFFAOYSA-N 0.000 description 2
- XJLXINKUBYWONI-NNYOXOHSSA-N NADP zwitterion Chemical compound NC(=O)C1=CC=C[N+]([C@H]2[C@@H]([C@H](O)[C@@H](COP([O-])(=O)OP(O)(=O)OC[C@@H]3[C@H]([C@@H](OP(O)(O)=O)[C@@H](O3)N3C4=NC=NC(N)=C4N=C3)O)O2)O)=C1 XJLXINKUBYWONI-NNYOXOHSSA-N 0.000 description 2
- 238000000692 Student's t-test Methods 0.000 description 2
- 150000001413 amino acids Chemical class 0.000 description 2
- 210000004102 animal cell Anatomy 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 239000012503 blood component Substances 0.000 description 2
- 210000001185 bone marrow Anatomy 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 238000004113 cell culture Methods 0.000 description 2
- 230000006037 cell lysis Effects 0.000 description 2
- 239000006285 cell suspension Substances 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- GNGACRATGGDKBX-UHFFFAOYSA-N dihydroxyacetone phosphate Chemical compound OCC(=O)COP(O)(O)=O GNGACRATGGDKBX-UHFFFAOYSA-N 0.000 description 2
- 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 2
- 239000003814 drug Substances 0.000 description 2
- 239000012520 frozen sample Substances 0.000 description 2
- 210000004072 lung Anatomy 0.000 description 2
- 238000012423 maintenance Methods 0.000 description 2
- 230000014759 maintenance of location Effects 0.000 description 2
- 229910052757 nitrogen Inorganic materials 0.000 description 2
- 239000012466 permeate Substances 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
- 229920003023 plastic Polymers 0.000 description 2
- 239000004033 plastic Substances 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 235000010344 sodium nitrate Nutrition 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- 230000004580 weight loss Effects 0.000 description 2
- QVHMXAMSRLOKNC-BTVCFUMJSA-N (2r,3s,4r,5r)-2,3,4,5,6-pentahydroxyhexanal;7h-purin-6-amine Chemical compound NC1=NC=NC2=C1NC=N2.OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C=O QVHMXAMSRLOKNC-BTVCFUMJSA-N 0.000 description 1
- INGWEZCOABYORO-UHFFFAOYSA-N 2-(furan-2-yl)-7-methyl-1h-1,8-naphthyridin-4-one Chemical compound N=1C2=NC(C)=CC=C2C(O)=CC=1C1=CC=CO1 INGWEZCOABYORO-UHFFFAOYSA-N 0.000 description 1
- RSGFPIWWSCWCFJ-VAXZQHAWSA-N 2-hydroxypropane-1,2,3-tricarboxylic acid;(2r,3s,4r,5r)-2,3,4,5,6-pentahydroxyhexanal;phosphoric acid Chemical compound OP(O)(O)=O.OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C=O.OC(=O)CC(O)(C(O)=O)CC(O)=O RSGFPIWWSCWCFJ-VAXZQHAWSA-N 0.000 description 1
- GHCZTIFQWKKGSB-UHFFFAOYSA-N 2-hydroxypropane-1,2,3-tricarboxylic acid;phosphoric acid Chemical compound OP(O)(O)=O.OC(=O)CC(O)(C(O)=O)CC(O)=O GHCZTIFQWKKGSB-UHFFFAOYSA-N 0.000 description 1
- LJQLQCAXBUHEAZ-UWTATZPHSA-N 3-phospho-D-glyceroyl dihydrogen phosphate Chemical compound OP(=O)(O)OC[C@@H](O)C(=O)OP(O)(O)=O LJQLQCAXBUHEAZ-UWTATZPHSA-N 0.000 description 1
- DZLBWVZPOJJFOH-GGWOSOGESA-N 4,5-bis[(e)-but-2-enoxy]imidazolidin-2-one Chemical compound C\C=C\COC1NC(=O)NC1OC\C=C\C DZLBWVZPOJJFOH-GGWOSOGESA-N 0.000 description 1
- PQGCEDQWHSBAJP-TXICZTDVSA-I 5-O-phosphonato-alpha-D-ribofuranosyl diphosphate(5-) Chemical compound O[C@H]1[C@@H](O)[C@@H](OP([O-])(=O)OP([O-])([O-])=O)O[C@@H]1COP([O-])([O-])=O PQGCEDQWHSBAJP-TXICZTDVSA-I 0.000 description 1
- 101100447462 Brugia malayi G3PD gene Proteins 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 206010018910 Haemolysis Diseases 0.000 description 1
- 241000155250 Iole Species 0.000 description 1
- JVTAAEKCZFNVCJ-UHFFFAOYSA-M Lactate Chemical compound CC(O)C([O-])=O JVTAAEKCZFNVCJ-UHFFFAOYSA-M 0.000 description 1
- 239000000232 Lipid Bilayer Substances 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- ACFIXJIJDZMPPO-NNYOXOHSSA-N NADPH 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](OP(O)(O)=O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 ACFIXJIJDZMPPO-NNYOXOHSSA-N 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 241000282320 Panthera leo Species 0.000 description 1
- 206010057249 Phagocytosis Diseases 0.000 description 1
- 108091006629 SLC13A2 Proteins 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 238000007818 agglutination assay Methods 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 239000012637 allosteric effector Substances 0.000 description 1
- 239000003146 anticoagulant agent Substances 0.000 description 1
- 229940127219 anticoagulant drug Drugs 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 102000036639 antigens Human genes 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- 230000006851 antioxidant defense Effects 0.000 description 1
- 235000010323 ascorbic acid Nutrition 0.000 description 1
- 229960005070 ascorbic acid Drugs 0.000 description 1
- 239000011668 ascorbic acid Substances 0.000 description 1
- 238000002306 biochemical method Methods 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 239000012888 bovine serum Substances 0.000 description 1
- 239000006172 buffering agent Substances 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 230000019522 cellular metabolic process Effects 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 230000002939 deleterious effect Effects 0.000 description 1
- 238000000432 density-gradient centrifugation Methods 0.000 description 1
- 108010002255 deoxyhemoglobin Proteins 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000003795 desorption Methods 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 238000009792 diffusion process Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- XPPKVPWEQAFLFU-UHFFFAOYSA-J diphosphate(4-) Chemical compound [O-]P([O-])(=O)OP([O-])([O-])=O XPPKVPWEQAFLFU-UHFFFAOYSA-J 0.000 description 1
- 235000011180 diphosphates Nutrition 0.000 description 1
- 150000002016 disaccharides Chemical class 0.000 description 1
- 210000003617 erythrocyte membrane Anatomy 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 230000006870 function Effects 0.000 description 1
- 102000018146 globin Human genes 0.000 description 1
- 108060003196 globin Proteins 0.000 description 1
- 150000002314 glycerols Chemical class 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 208000034737 hemoglobinopathy Diseases 0.000 description 1
- 230000008588 hemolysis Effects 0.000 description 1
- 210000004754 hybrid cell Anatomy 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 238000012417 linear regression Methods 0.000 description 1
- 230000003859 lipid peroxidation Effects 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 230000004792 oxidative damage Effects 0.000 description 1
- KLAKIAVEMQMVBT-UHFFFAOYSA-N p-hydroxy-phenacyl alcohol Natural products OCC(=O)C1=CC=C(O)C=C1 KLAKIAVEMQMVBT-UHFFFAOYSA-N 0.000 description 1
- 230000004108 pentose phosphate pathway Effects 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 230000008782 phagocytosis Effects 0.000 description 1
- 229920001983 poloxamer Polymers 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 210000001938 protoplast Anatomy 0.000 description 1
- 239000000700 radioactive tracer Substances 0.000 description 1
- 238000009790 rate-determining step (RDS) Methods 0.000 description 1
- WPPDXAHGCGPUPK-UHFFFAOYSA-N red 2 Chemical compound C1=CC=CC=C1C(C1=CC=CC=C11)=C(C=2C=3C4=CC=C5C6=CC=C7C8=C(C=9C=CC=CC=9)C9=CC=CC=C9C(C=9C=CC=CC=9)=C8C8=CC=C(C6=C87)C(C=35)=CC=2)C4=C1C1=CC=CC=C1 WPPDXAHGCGPUPK-UHFFFAOYSA-N 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000013049 sediment Substances 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- PXLIDIMHPNPGMH-UHFFFAOYSA-N sodium chromate Chemical compound [Na+].[Na+].[O-][Cr]([O-])(=O)=O PXLIDIMHPNPGMH-UHFFFAOYSA-N 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000010257 thawing Methods 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000035899 viability Effects 0.000 description 1
- 238000003260 vortexing Methods 0.000 description 1
- 210000000707 wrist Anatomy 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01N—PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTS THEREOF; BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES OR AS HERBICIDES; PEST REPELLANTS OR ATTRACTANTS; PLANT GROWTH REGULATORS
- A01N1/00—Preservation of bodies of humans or animals, or parts thereof
- A01N1/02—Preservation of living parts
- A01N1/0205—Chemical aspects
- A01N1/021—Preservation or perfusion media, liquids, solids or gases used in the preservation of cells, tissue, organs or bodily fluids
- A01N1/0221—Freeze-process protecting agents, i.e. substances protecting cells from effects of the physical process, e.g. cryoprotectants, osmolarity regulators like oncotic agents
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01N—PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTS THEREOF; BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES OR AS HERBICIDES; PEST REPELLANTS OR ATTRACTANTS; PLANT GROWTH REGULATORS
- A01N1/00—Preservation of bodies of humans or animals, or parts thereof
- A01N1/02—Preservation of living parts
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K35/00—Medicinal preparations containing materials or reaction products thereof with undetermined constitution
- A61K35/12—Materials from mammals; Compositions comprising non-specified tissues or cells; Compositions comprising non-embryonic stem cells; Genetically modified cells
- A61K35/14—Blood; Artificial blood
- A61K35/18—Erythrocytes
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Environmental Sciences (AREA)
- Wood Science & Technology (AREA)
- Dentistry (AREA)
- Medicinal Chemistry (AREA)
- Animal Behavior & Ethology (AREA)
- Immunology (AREA)
- Chemical & Material Sciences (AREA)
- Developmental Biology & Embryology (AREA)
- Pharmacology & Pharmacy (AREA)
- Epidemiology (AREA)
- Virology (AREA)
- Cell Biology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Hematology (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US52895590A | 1990-05-25 | 1990-05-25 | |
| US528,955 | 1990-05-25 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2062941A1 true CA2062941A1 (fr) | 1991-11-26 |
Family
ID=24107917
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002062941A Abandoned CA2062941A1 (fr) | 1990-05-25 | 1991-05-24 | Procede pour lyophiliser les cellules, matieres et plaquettes de type cellules dans un melange de polymeres amphipatiques biocompatibles |
Country Status (7)
| Country | Link |
|---|---|
| EP (1) | EP0484519A4 (fr) |
| JP (1) | JPH05501419A (fr) |
| AU (1) | AU8064691A (fr) |
| CA (1) | CA2062941A1 (fr) |
| IL (1) | IL98269A0 (fr) |
| WO (1) | WO1991018504A1 (fr) |
| ZA (1) | ZA913995B (fr) |
Families Citing this family (23)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| IL90188A0 (en) * | 1988-05-18 | 1989-12-15 | Cryopharm Corp | Process and medium for the lyophilization of erythrocytes |
| US5045446A (en) * | 1988-08-26 | 1991-09-03 | Cryopharm Corporation | Lyophilization of cells |
| US5213814A (en) * | 1989-04-10 | 1993-05-25 | Cryopharm Corporation | Lyophilized and reconstituted blood platelet compositions |
| AU650045B2 (en) * | 1990-09-12 | 1994-06-09 | Lifecell Corporation | Method and apparatus for cryopreparation dry stabilization and rehydration of biological suspensions |
| US5336616A (en) * | 1990-09-12 | 1994-08-09 | Lifecell Corporation | Method for processing and preserving collagen-based tissues for transplantation |
| US8067149B2 (en) | 1990-09-12 | 2011-11-29 | Lifecell Corporation | Acellular dermal matrix and method of use thereof for grafting |
| US6060233A (en) * | 1996-06-14 | 2000-05-09 | Biostore New Zealand, Ltd | Methods for the lyophilization of platelets, platelet membranes or erythrocytes |
| US6037116A (en) * | 1996-06-14 | 2000-03-14 | Biostore New Zealand, Ltd. | Compositions comprising betaine, sodium citrate and sodium chloride and methods for the preservation of biological materials |
| WO1997047192A1 (fr) * | 1996-06-14 | 1997-12-18 | Biostore New Zealand Limited | Compositions et procedes de conservation de tissus vivants |
| US6361933B1 (en) | 1996-06-14 | 2002-03-26 | Biostore New Zealand Limited | Solutions for the preservation of tissues |
| US6114107A (en) * | 1996-06-14 | 2000-09-05 | Biostore New Zealand Limited | Composition comprising raffinose, TMAO, sodium citrate and methods for the preservation of living tissues |
| US5827640A (en) * | 1996-06-14 | 1998-10-27 | Biostore New Zealand Limited | Methods for the preservation of cells and tissues using trimethylamine oxide or betaine with raffinose or trehalose |
| US5879875A (en) * | 1996-06-14 | 1999-03-09 | Biostore New Zealand | Compositions and methods for the preservation of living tissues |
| US6040132A (en) * | 1996-06-14 | 2000-03-21 | Biostore New Zealand, Ltd. | Methods for the lyophilization of living biological materials |
| US5962213A (en) * | 1996-06-14 | 1999-10-05 | Biostore New Zealand Limited | Compositions and methods for the preservation of living tissues |
| US6743575B2 (en) | 1996-06-14 | 2004-06-01 | Biostore New Zealand Ltd. | Compositions and methods for the preservation of living tissues |
| ATE316757T1 (de) | 1998-05-26 | 2006-02-15 | Lifecell Corp | Cryokonservierung menschlicher roter blutzellen |
| US6933326B1 (en) | 1998-06-19 | 2005-08-23 | Lifecell Coporation | Particulate acellular tissue matrix |
| US7112576B1 (en) | 1999-12-10 | 2006-09-26 | Regents Of The University Of Minnesota | Compositions and methods for cryopreservation of peripheral blood lymphocytes |
| JP2002226368A (ja) * | 2001-02-02 | 2002-08-14 | Fuji Chem Ind Co Ltd | 赤血球の酸化的損傷抑制剤 |
| GB0230152D0 (en) * | 2002-12-24 | 2003-02-05 | Sinvent As | Product |
| EP1929289B1 (fr) | 2005-09-26 | 2018-02-21 | Lifecell Corporation | Composition de plaquettes dessechees |
| KR101410065B1 (ko) * | 2011-12-09 | 2014-06-27 | 테고사이언스 (주) | 세포의 유용물질을 상온에서 안정하게 보존하는 방법 |
Family Cites Families (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3303662A (en) * | 1963-03-01 | 1967-02-14 | Union Carbide Corp | Process for cell preservation |
| BE643051A (fr) * | 1963-05-31 | 1964-05-15 | ||
| US3915794A (en) * | 1973-02-09 | 1975-10-28 | Rit Rech Ind Therapeut | Stabilizing compositions for cell-free viruses and cell-free virus preparations containing them |
| DE2310964A1 (de) * | 1973-03-02 | 1974-09-05 | Schering Ag | Antigen- bzw. antigen-proteinkonjugatbeschichtete erythrocytenpraeparation |
| US4963362A (en) * | 1987-08-07 | 1990-10-16 | Regents Of The University Of Minnesota | Freeze-dried liposome mixture containing cyclosporin |
| US5213814A (en) * | 1989-04-10 | 1993-05-25 | Cryopharm Corporation | Lyophilized and reconstituted blood platelet compositions |
| US5045446A (en) * | 1988-08-26 | 1991-09-03 | Cryopharm Corporation | Lyophilization of cells |
| IL90188A0 (en) * | 1988-05-18 | 1989-12-15 | Cryopharm Corp | Process and medium for the lyophilization of erythrocytes |
| US5178884A (en) * | 1988-05-18 | 1993-01-12 | Cryopharm Corporation | Lyophilized and reconstituted red blood cell compositions |
| US4874690A (en) * | 1988-08-26 | 1989-10-17 | Cryopharm Corporation | Lyophilization of red blood cells |
| WO1991016060A1 (fr) * | 1990-04-16 | 1991-10-31 | Cryopharm Corporation | Procede pour rendre inactifs des contaminants sanguins viraux et bacteriens |
| AU1415992A (en) * | 1991-02-15 | 1992-09-15 | Cryopharm Corporation | Method of lyophilization and reconstitution of mixtures of nucleated non-mammalian cells and blood matter |
-
1991
- 1991-05-24 WO PCT/US1991/003544 patent/WO1991018504A1/fr not_active Application Discontinuation
- 1991-05-24 CA CA002062941A patent/CA2062941A1/fr not_active Abandoned
- 1991-05-24 EP EP19910912119 patent/EP0484519A4/en not_active Withdrawn
- 1991-05-24 AU AU80646/91A patent/AU8064691A/en not_active Abandoned
- 1991-05-24 JP JP3511192A patent/JPH05501419A/ja active Pending
- 1991-05-26 IL IL98269A patent/IL98269A0/xx unknown
- 1991-05-27 ZA ZA913995A patent/ZA913995B/xx unknown
Also Published As
| Publication number | Publication date |
|---|---|
| EP0484519A1 (fr) | 1992-05-13 |
| ZA913995B (en) | 1992-03-25 |
| AU8064691A (en) | 1991-12-31 |
| JPH05501419A (ja) | 1993-03-18 |
| WO1991018504A1 (fr) | 1991-12-12 |
| IL98269A0 (en) | 1992-06-21 |
| EP0484519A4 (en) | 1993-12-29 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CA2062941A1 (fr) | Procede pour lyophiliser les cellules, matieres et plaquettes de type cellules dans un melange de polymeres amphipatiques biocompatibles | |
| CA1327763C (fr) | Lyophilisation de cellules | |
| US5043261A (en) | Lyophilized and reconstituted red blood cell and hemosome compositions | |
| US5213814A (en) | Lyophilized and reconstituted blood platelet compositions | |
| US5340592A (en) | Lyophilization of erythrocytes | |
| Högman et al. | Storage parameters affecting red blood cell survival and function after transfusion | |
| US4874690A (en) | Lyophilization of red blood cells | |
| US4695460A (en) | Synthetic, plasma-free, transfusible platelet storage medium | |
| EP0392813A2 (fr) | Procédé de reconstitution d'érythrocytes et/ou d'hémosomes lyophilisés | |
| AU3443093A (en) | Method of freezing cells and cell-like materials | |
| US5171661A (en) | Medium for lyophilization of erythrocytes | |
| US5153004A (en) | Freezing and thawing of erythrocytes | |
| US5690963A (en) | Freeze dried red blood cells | |
| Moroff et al. | Characterization of biochemical changes occurring during storage of red cells: Comparative studies with CPD and CPDA‐1 anticoagulant‐preservative solutions | |
| WO1993000806A1 (fr) | Deshydratation de cellules sanguines et procede de preparation | |
| Hess et al. | Buffering and dilution in red blood cell storage | |
| Herve et al. | Preservation of human erythrocytes in the liquid state: biological results with a new medium | |
| US20070105220A1 (en) | Erythrocytic cells and method for loading solutes | |
| Weinstein et al. | Survival of lyophilized and reconstituted human red blood cells in vivo | |
| Moore et al. | The distribution and utilization of adenine in red blood cells during 42 days of 4 C storage | |
| Franco et al. | The 24‐Hour Posttransfusion Survival and Lifespan of Autologous Baboon Red Cells Treated with Inositol Hexaphosphate‐Polyethylene Glycol or Inositol Hexaphosphate‐Adenosine Triphosphate‐Polyethylene Glycol to Decrease Oxygen Affinity 1 | |
| Derrick et al. | Studies of the Metabolic Integrity of Human Red Blood Cells After Cryopreservation: II. Effects of Low‐glycerol‐Rapid‐freeze Preservation on Glycolysis | |
| Castro | Cryopreservation of cyanate-treated sickle erythrocytes | |
| Castro et al. | Autologous survival of cyanate‐treated cryopreserved sickle erythrocytes | |
| Wrotnowski et al. | Evaluation of Adenosine Triphosphate and 2, 3-Diphosphogly cerate after Twenty-Four Hours in Red Cells Washed for Neonatal Transfusion |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FZDE | Discontinued |