SK3042000A3 - Transgenic mammals which produce oligosaccharides in their milk - Google Patents
Transgenic mammals which produce oligosaccharides in their milk Download PDFInfo
- Publication number
- SK3042000A3 SK3042000A3 SK304-2000A SK3042000A SK3042000A3 SK 3042000 A3 SK3042000 A3 SK 3042000A3 SK 3042000 A SK3042000 A SK 3042000A SK 3042000 A3 SK3042000 A3 SK 3042000A3
- Authority
- SK
- Slovakia
- Prior art keywords
- lacto
- fucopentaose
- derivative
- milk
- sialylated
- Prior art date
Links
- 150000002482 oligosaccharides Chemical class 0.000 title claims abstract description 153
- 229920001542 oligosaccharide Polymers 0.000 title claims abstract description 152
- 230000009261 transgenic effect Effects 0.000 title claims abstract description 135
- 235000013336 milk Nutrition 0.000 title claims abstract description 123
- 239000008267 milk Substances 0.000 title claims abstract description 123
- 210000004080 milk Anatomy 0.000 title claims abstract description 123
- 241000124008 Mammalia Species 0.000 title claims abstract description 41
- 238000000034 method Methods 0.000 claims abstract description 53
- 239000000203 mixture Substances 0.000 claims abstract description 13
- 102000004190 Enzymes Human genes 0.000 claims description 67
- 108090000790 Enzymes Proteins 0.000 claims description 67
- 230000014509 gene expression Effects 0.000 claims description 40
- 108700023372 Glycosyltransferases Proteins 0.000 claims description 39
- 108700019146 Transgenes Proteins 0.000 claims description 38
- 102000003886 Glycoproteins Human genes 0.000 claims description 36
- 108090000288 Glycoproteins Proteins 0.000 claims description 36
- 241000699666 Mus <mouse, genus> Species 0.000 claims description 32
- 229930193965 lacto-N-fucopentaose Natural products 0.000 claims description 30
- 238000004519 manufacturing process Methods 0.000 claims description 28
- 241000283973 Oryctolagus cuniculus Species 0.000 claims description 22
- AUNPEJDACLEKSC-ZAYDSPBTSA-N 3-fucosyllactose Chemical compound O[C@H]1[C@H](O)[C@H](O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](O)[C@H](O[C@@H]2[C@H](OC(O)[C@H](O)[C@H]2O)CO)O[C@H](CO)[C@@H]1O AUNPEJDACLEKSC-ZAYDSPBTSA-N 0.000 claims description 20
- SNFSYLYCDAVZGP-UHFFFAOYSA-N UNPD26986 Natural products OC1C(O)C(O)C(C)OC1OC1C(OC2C(OC(O)C(O)C2O)CO)OC(CO)C(O)C1O SNFSYLYCDAVZGP-UHFFFAOYSA-N 0.000 claims description 20
- 102000051366 Glycosyltransferases Human genes 0.000 claims description 16
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 16
- 229940062827 2'-fucosyllactose Drugs 0.000 claims description 12
- HWHQUWQCBPAQQH-UHFFFAOYSA-N 2-O-alpha-L-Fucosyl-lactose Natural products OC1C(O)C(O)C(C)OC1OC1C(O)C(O)C(CO)OC1OC(C(O)CO)C(O)C(O)C=O HWHQUWQCBPAQQH-UHFFFAOYSA-N 0.000 claims description 12
- HWHQUWQCBPAQQH-BWRPKUOHSA-N 2-fucosyllactose Chemical compound O[C@H]1[C@H](O)[C@H](O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@H]([C@H](O)CO)[C@H](O)[C@@H](O)C=O HWHQUWQCBPAQQH-BWRPKUOHSA-N 0.000 claims description 12
- 108010019236 Fucosyltransferases Proteins 0.000 claims description 12
- 102000006471 Fucosyltransferases Human genes 0.000 claims description 12
- 102000006722 Mannosyltransferases Human genes 0.000 claims description 12
- 108010087568 Mannosyltransferases Proteins 0.000 claims description 12
- 239000008103 glucose Substances 0.000 claims description 12
- 210000004027 cell Anatomy 0.000 claims description 11
- 210000005075 mammary gland Anatomy 0.000 claims description 11
- 210000001161 mammalian embryo Anatomy 0.000 claims description 10
- 241000283707 Capra Species 0.000 claims description 9
- PDWGIAAFQACISG-QZBWVFMZSA-N beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-[beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->6)]-beta-D-Gal-(1->4)-D-Glc Chemical compound O([C@H]1[C@H](O)[C@H]([C@@H](O[C@@H]1CO)OC[C@@H]1[C@@H]([C@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O3)O)[C@H](O)[C@@H](CO)O2)NC(C)=O)[C@@H](O)[C@H](O[C@@H]2[C@H](OC(O)[C@H](O)[C@H]2O)CO)O1)O)NC(=O)C)[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O PDWGIAAFQACISG-QZBWVFMZSA-N 0.000 claims description 9
- 241000283690 Bos taurus Species 0.000 claims description 8
- 235000016709 nutrition Nutrition 0.000 claims description 8
- 102000030902 Galactosyltransferase Human genes 0.000 claims description 7
- 108060003306 Galactosyltransferase Proteins 0.000 claims description 7
- 241000282898 Sus scrofa Species 0.000 claims description 7
- CMQZRJBJDCVIEY-JEOLMMCMSA-N alpha-L-Fucp-(1->3)-[beta-D-Galp-(1->4)]-beta-D-GlcpNAc-(1->3)-beta-D-Galp-(1->4)-D-Glcp Chemical compound O[C@H]1[C@H](O)[C@H](O)[C@H](C)O[C@H]1O[C@H]1[C@H](O[C@H]2[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O2)O)[C@@H](CO)O[C@@H](O[C@@H]2[C@H]([C@H](O[C@@H]3[C@H](OC(O)[C@H](O)[C@H]3O)CO)O[C@H](CO)[C@@H]2O)O)[C@@H]1NC(C)=O CMQZRJBJDCVIEY-JEOLMMCMSA-N 0.000 claims description 7
- 235000013350 formula milk Nutrition 0.000 claims description 7
- CMQZRJBJDCVIEY-UHFFFAOYSA-N lacto-N-fucopentaose III Natural products OC1C(O)C(O)C(C)OC1OC1C(OC2C(C(O)C(O)C(CO)O2)O)C(CO)OC(OC2C(C(OC3C(OC(O)C(O)C3O)CO)OC(CO)C2O)O)C1NC(C)=O CMQZRJBJDCVIEY-UHFFFAOYSA-N 0.000 claims description 7
- 108010013043 Acetylesterase Proteins 0.000 claims description 6
- 241001494479 Pecora Species 0.000 claims description 6
- 241000700159 Rattus Species 0.000 claims description 6
- DUKURNFHYQXCJG-JEOLMMCMSA-N alpha-L-Fucp-(1->4)-[beta-D-Galp-(1->3)]-beta-D-GlcpNAc-(1->3)-beta-D-Galp-(1->4)-D-Glcp Chemical compound O[C@H]1[C@H](O)[C@H](O)[C@H](C)O[C@H]1O[C@H]1[C@H](O[C@H]2[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O2)O)[C@@H](NC(C)=O)[C@H](O[C@@H]2[C@H]([C@H](O[C@@H]3[C@H](OC(O)[C@H](O)[C@H]3O)CO)O[C@H](CO)[C@@H]2O)O)O[C@@H]1CO DUKURNFHYQXCJG-JEOLMMCMSA-N 0.000 claims description 6
- 229930182830 galactose Natural products 0.000 claims description 6
- -1 gluconyllepimerase Proteins 0.000 claims description 6
- FKADDOYBRRMBPP-UHFFFAOYSA-N lacto-N-fucopentaose II Natural products OC1C(O)C(O)C(C)OC1OC1C(OC2C(C(O)C(O)C(CO)O2)O)C(NC(C)=O)C(OC2C(C(OC(C(O)CO)C(O)C(O)C=O)OC(CO)C2O)O)OC1CO FKADDOYBRRMBPP-UHFFFAOYSA-N 0.000 claims description 6
- 210000002955 secretory cell Anatomy 0.000 claims description 6
- 102000016354 Glucuronosyltransferase Human genes 0.000 claims description 5
- 108010092364 Glucuronosyltransferase Proteins 0.000 claims description 5
- TVVLIFCVJJSLBL-SEHWTJTBSA-N Lacto-N-fucopentaose V Chemical compound O[C@H]1C(O)C(O)[C@H](C)O[C@H]1OC([C@@H](O)C=O)[C@@H](C(O)CO)O[C@H]1[C@H](O)[C@@H](OC2[C@@H](C(OC3[C@@H](C(O)C(O)[C@@H](CO)O3)O)[C@H](O)[C@@H](CO)O2)NC(C)=O)[C@@H](O)[C@@H](CO)O1 TVVLIFCVJJSLBL-SEHWTJTBSA-N 0.000 claims description 5
- 102000004357 Transferases Human genes 0.000 claims description 5
- 108090000992 Transferases Proteins 0.000 claims description 5
- AXQLFFDZXPOFPO-UHFFFAOYSA-N UNPD216 Natural products O1C(CO)C(O)C(OC2C(C(O)C(O)C(CO)O2)O)C(NC(=O)C)C1OC(C1O)C(O)C(CO)OC1OC1C(O)C(O)C(O)OC1CO AXQLFFDZXPOFPO-UHFFFAOYSA-N 0.000 claims description 5
- AXQLFFDZXPOFPO-UNTPKZLMSA-N beta-D-Galp-(1->3)-beta-D-GlcpNAc-(1->3)-beta-D-Galp-(1->4)-beta-D-Glcp Chemical compound O([C@@H]1O[C@H](CO)[C@H](O)[C@@H]([C@H]1O)O[C@H]1[C@@H]([C@H]([C@H](O)[C@@H](CO)O1)O[C@H]1[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O1)O)NC(=O)C)[C@H]1[C@H](O)[C@@H](O)[C@H](O)O[C@@H]1CO AXQLFFDZXPOFPO-UNTPKZLMSA-N 0.000 claims description 5
- IEQCXFNWPAHHQR-UHFFFAOYSA-N lacto-N-neotetraose Natural products OCC1OC(OC2C(C(OC3C(OC(O)C(O)C3O)CO)OC(CO)C2O)O)C(NC(=O)C)C(O)C1OC1OC(CO)C(O)C(O)C1O IEQCXFNWPAHHQR-UHFFFAOYSA-N 0.000 claims description 5
- USIPEGYTBGEPJN-UHFFFAOYSA-N lacto-N-tetraose Natural products O1C(CO)C(O)C(OC2C(C(O)C(O)C(CO)O2)O)C(NC(=O)C)C1OC1C(O)C(CO)OC(OC(C(O)CO)C(O)C(O)C=O)C1O USIPEGYTBGEPJN-UHFFFAOYSA-N 0.000 claims description 5
- 229940062780 lacto-n-neotetraose Drugs 0.000 claims description 5
- KFOPKOFKGJJEBW-ZSSYTAEJSA-N methyl 2-[(1s,7r,8s,9s,10r,13r,14s,17r)-1,7-dihydroxy-10,13-dimethyl-3-oxo-1,2,6,7,8,9,11,12,14,15,16,17-dodecahydrocyclopenta[a]phenanthren-17-yl]acetate Chemical compound C([C@H]1O)C2=CC(=O)C[C@H](O)[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H](CC(=O)OC)[C@@]1(C)CC2 KFOPKOFKGJJEBW-ZSSYTAEJSA-N 0.000 claims description 5
- RBMYDHMFFAVMMM-PLQWBNBWSA-N neolactotetraose Chemical compound O([C@H]1[C@H](O)[C@H]([C@@H](O[C@@H]1CO)O[C@@H]1[C@H]([C@H](O[C@H]([C@H](O)CO)[C@H](O)[C@@H](O)C=O)O[C@H](CO)[C@@H]1O)O)NC(=O)C)[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O RBMYDHMFFAVMMM-PLQWBNBWSA-N 0.000 claims description 5
- 102000003838 Sialyltransferases Human genes 0.000 claims description 4
- 108090000141 Sialyltransferases Proteins 0.000 claims description 4
- 230000001105 regulatory effect Effects 0.000 claims description 4
- 108091026890 Coding region Proteins 0.000 claims description 3
- 108010076504 Protein Sorting Signals Proteins 0.000 claims description 3
- 102000004896 Sulfotransferases Human genes 0.000 claims description 3
- 108090001033 Sulfotransferases Proteins 0.000 claims description 3
- 239000007787 solid Substances 0.000 claims description 3
- 239000007788 liquid Substances 0.000 claims description 2
- 230000035764 nutrition Effects 0.000 claims description 2
- 230000000392 somatic effect Effects 0.000 claims description 2
- 102000000340 Glucosyltransferases Human genes 0.000 claims 4
- 108010055629 Glucosyltransferases Proteins 0.000 claims 4
- 102000005421 acetyltransferase Human genes 0.000 claims 3
- 108020002494 acetyltransferase Proteins 0.000 claims 3
- 229930006000 Sucrose Natural products 0.000 claims 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 claims 1
- 239000005720 sucrose Substances 0.000 claims 1
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 66
- 239000000523 sample Substances 0.000 description 60
- 229940088598 enzyme Drugs 0.000 description 58
- 108090000623 proteins and genes Proteins 0.000 description 41
- 241001465754 Metazoa Species 0.000 description 32
- 239000000284 extract Substances 0.000 description 26
- 102000045442 glycosyltransferase activity proteins Human genes 0.000 description 23
- 108700014210 glycosyltransferase activity proteins Proteins 0.000 description 23
- 238000004458 analytical method Methods 0.000 description 22
- 102000004169 proteins and genes Human genes 0.000 description 21
- HNSDLXPSAYFUHK-UHFFFAOYSA-N 1,4-bis(2-ethylhexyl) sulfosuccinate Chemical compound CCCCC(CC)COC(=O)CC(S(O)(=O)=O)C(=O)OCC(CC)CCCC HNSDLXPSAYFUHK-UHFFFAOYSA-N 0.000 description 19
- 235000018102 proteins Nutrition 0.000 description 19
- 239000000499 gel Substances 0.000 description 18
- 150000004043 trisaccharides Chemical class 0.000 description 18
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 18
- WJPIUUDKRHCAEL-UHFFFAOYSA-N 3FL Natural products OC1C(O)C(O)C(C)OC1OC1C(OC2C(C(O)C(O)C(CO)O2)O)C(CO)OC(O)C1O WJPIUUDKRHCAEL-UHFFFAOYSA-N 0.000 description 14
- 108020004414 DNA Proteins 0.000 description 13
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 13
- 241000699670 Mus sp. Species 0.000 description 13
- 238000010828 elution Methods 0.000 description 11
- 239000000047 product Substances 0.000 description 11
- 230000015572 biosynthetic process Effects 0.000 description 10
- 239000002299 complementary DNA Substances 0.000 description 10
- 238000003786 synthesis reaction Methods 0.000 description 10
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 9
- 102000012086 alpha-L-Fucosidase Human genes 0.000 description 9
- 108010061314 alpha-L-Fucosidase Proteins 0.000 description 9
- 238000001962 electrophoresis Methods 0.000 description 9
- 239000008101 lactose Substances 0.000 description 9
- 230000007935 neutral effect Effects 0.000 description 9
- 239000013612 plasmid Substances 0.000 description 9
- 238000012250 transgenic expression Methods 0.000 description 9
- SNFSYLYCDAVZGP-OLAZETNGSA-N 2'-fucosyllactose Chemical compound O[C@H]1[C@H](O)[C@H](O)[C@H](C)O[C@H]1O[C@H]1[C@H](O[C@@H]2[C@H](OC(O)[C@H](O)[C@H]2O)CO)O[C@H](CO)[C@H](O)[C@@H]1O SNFSYLYCDAVZGP-OLAZETNGSA-N 0.000 description 8
- 101710188695 Alpha-(1,3)-fucosyltransferase 4 Proteins 0.000 description 8
- 102100035248 Alpha-(1,3)-fucosyltransferase 4 Human genes 0.000 description 8
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 8
- 150000001720 carbohydrates Chemical class 0.000 description 8
- 235000014633 carbohydrates Nutrition 0.000 description 8
- 239000003153 chemical reaction reagent Substances 0.000 description 8
- 239000000463 material Substances 0.000 description 8
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 7
- 230000001580 bacterial effect Effects 0.000 description 7
- 230000008488 polyadenylation Effects 0.000 description 7
- 239000013598 vector Substances 0.000 description 7
- 239000012901 Milli-Q water Substances 0.000 description 6
- 230000009471 action Effects 0.000 description 6
- 238000005571 anion exchange chromatography Methods 0.000 description 6
- 238000010790 dilution Methods 0.000 description 6
- 239000012895 dilution Substances 0.000 description 6
- 239000012634 fragment Substances 0.000 description 6
- 230000010354 integration Effects 0.000 description 6
- 230000006651 lactation Effects 0.000 description 6
- 210000001519 tissue Anatomy 0.000 description 6
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 5
- 108010006025 bovine growth hormone Proteins 0.000 description 5
- 230000001983 lactogenic effect Effects 0.000 description 5
- 238000002360 preparation method Methods 0.000 description 5
- 230000008569 process Effects 0.000 description 5
- 239000000243 solution Substances 0.000 description 5
- 241000894007 species Species 0.000 description 5
- 235000000346 sugar Nutrition 0.000 description 5
- SHZGCJCMOBCMKK-UHFFFAOYSA-N D-mannomethylose Natural products CC1OC(O)C(O)C(O)C1O SHZGCJCMOBCMKK-UHFFFAOYSA-N 0.000 description 4
- 241000282412 Homo Species 0.000 description 4
- 229920002472 Starch Polymers 0.000 description 4
- 239000005862 Whey Substances 0.000 description 4
- 102000007544 Whey Proteins Human genes 0.000 description 4
- 108010046377 Whey Proteins Proteins 0.000 description 4
- 239000002253 acid Substances 0.000 description 4
- 150000001450 anions Chemical class 0.000 description 4
- 239000000427 antigen Substances 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- 239000013068 control sample Substances 0.000 description 4
- 235000013365 dairy product Nutrition 0.000 description 4
- 230000029087 digestion Effects 0.000 description 4
- 238000001035 drying Methods 0.000 description 4
- 210000002257 embryonic structure Anatomy 0.000 description 4
- 230000002068 genetic effect Effects 0.000 description 4
- 238000003384 imaging method Methods 0.000 description 4
- 239000012528 membrane Substances 0.000 description 4
- 239000002953 phosphate buffered saline Substances 0.000 description 4
- 239000001632 sodium acetate Substances 0.000 description 4
- 235000017281 sodium acetate Nutrition 0.000 description 4
- 235000019698 starch Nutrition 0.000 description 4
- 239000008107 starch Substances 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- 238000012546 transfer Methods 0.000 description 4
- 238000011830 transgenic mouse model Methods 0.000 description 4
- 102000011022 Chorionic Gonadotropin Human genes 0.000 description 3
- 108010062540 Chorionic Gonadotropin Proteins 0.000 description 3
- PNNNRSAQSRJVSB-SLPGGIOYSA-N Fucose Natural products C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)C=O PNNNRSAQSRJVSB-SLPGGIOYSA-N 0.000 description 3
- SHZGCJCMOBCMKK-DHVFOXMCSA-N L-fucopyranose Chemical compound C[C@@H]1OC(O)[C@@H](O)[C@H](O)[C@@H]1O SHZGCJCMOBCMKK-DHVFOXMCSA-N 0.000 description 3
- 102000014171 Milk Proteins Human genes 0.000 description 3
- 108010011756 Milk Proteins Proteins 0.000 description 3
- 102100023315 N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase Human genes 0.000 description 3
- 108010056664 N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase Proteins 0.000 description 3
- YXFVVABEGXRONW-UHFFFAOYSA-N Toluene Chemical compound CC1=CC=CC=C1 YXFVVABEGXRONW-UHFFFAOYSA-N 0.000 description 3
- 108010090473 UDP-N-acetylglucosamine-peptide beta-N-acetylglucosaminyltransferase Proteins 0.000 description 3
- 108091007433 antigens Proteins 0.000 description 3
- 102000036639 antigens Human genes 0.000 description 3
- 210000004369 blood Anatomy 0.000 description 3
- 239000008280 blood Substances 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
- 238000012512 characterization method Methods 0.000 description 3
- 238000004587 chromatography analysis Methods 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 239000000469 ethanolic extract Substances 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 238000000605 extraction Methods 0.000 description 3
- 239000000706 filtrate Substances 0.000 description 3
- 238000001502 gel electrophoresis Methods 0.000 description 3
- 229940084986 human chorionic gonadotropin Drugs 0.000 description 3
- 235000020256 human milk Nutrition 0.000 description 3
- 238000002347 injection Methods 0.000 description 3
- 239000007924 injection Substances 0.000 description 3
- 230000009027 insemination Effects 0.000 description 3
- 235000021239 milk protein Nutrition 0.000 description 3
- 239000013642 negative control Substances 0.000 description 3
- 239000008188 pellet Substances 0.000 description 3
- 229920002401 polyacrylamide Polymers 0.000 description 3
- 238000001243 protein synthesis Methods 0.000 description 3
- 230000014616 translation Effects 0.000 description 3
- YGEHCIVVZVBCLE-FSYGUOKUSA-N 3alpha-galactobiose Chemical compound OC[C@@H](O)[C@H](O)[C@@H]([C@@H](O)C=O)O[C@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O YGEHCIVVZVBCLE-FSYGUOKUSA-N 0.000 description 2
- 101710105077 Agglutinin-1 Proteins 0.000 description 2
- 101710098620 Alpha-1,2-fucosyltransferase Proteins 0.000 description 2
- 108020004705 Codon Proteins 0.000 description 2
- 101150082479 GAL gene Proteins 0.000 description 2
- 229930186217 Glycolipid Natural products 0.000 description 2
- 101001022185 Homo sapiens Alpha-(1,3)-fucosyltransferase 4 Proteins 0.000 description 2
- 102000004407 Lactalbumin Human genes 0.000 description 2
- 108090000942 Lactalbumin Proteins 0.000 description 2
- 101100194625 Rattus norvegicus Rgs19 gene Proteins 0.000 description 2
- 206010042573 Superovulation Diseases 0.000 description 2
- 101001089018 Ulex europaeus Anti-H(O) lectin 1 Proteins 0.000 description 2
- 239000000370 acceptor Substances 0.000 description 2
- 239000008351 acetate buffer Substances 0.000 description 2
- 238000012511 carbohydrate analysis Methods 0.000 description 2
- 239000005018 casein Substances 0.000 description 2
- 230000003197 catalytic effect Effects 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 239000006071 cream Substances 0.000 description 2
- 239000003480 eluent Substances 0.000 description 2
- 125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 2
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 2
- 239000010931 gold Substances 0.000 description 2
- 229910052737 gold Inorganic materials 0.000 description 2
- 210000004251 human milk Anatomy 0.000 description 2
- 235000021244 human milk protein Nutrition 0.000 description 2
- 238000009396 hybridization Methods 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 230000001939 inductive effect Effects 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 210000004185 liver Anatomy 0.000 description 2
- 238000000520 microinjection Methods 0.000 description 2
- 150000002772 monosaccharides Chemical group 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 210000003101 oviduct Anatomy 0.000 description 2
- 229920000642 polymer Polymers 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- GAPYKZAARZMMGP-UHFFFAOYSA-N pyridin-1-ium;acetate Chemical compound CC(O)=O.C1=CC=NC=C1 GAPYKZAARZMMGP-UHFFFAOYSA-N 0.000 description 2
- 150000008163 sugars Chemical class 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 230000002103 transcriptional effect Effects 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- 238000001262 western blot Methods 0.000 description 2
- 210000002268 wool Anatomy 0.000 description 2
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- JVIPLYCGEZUBIO-UHFFFAOYSA-N 2-(4-fluorophenyl)-1,3-dioxoisoindole-5-carboxylic acid Chemical compound O=C1C2=CC(C(=O)O)=CC=C2C(=O)N1C1=CC=C(F)C=C1 JVIPLYCGEZUBIO-UHFFFAOYSA-N 0.000 description 1
- 108010083651 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase Proteins 0.000 description 1
- 101710147124 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3 Proteins 0.000 description 1
- QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 1
- 101000893749 Arabidopsis thaliana Alpha-L-fucosidase 3 Proteins 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 208000035143 Bacterial infection Diseases 0.000 description 1
- 235000018185 Betula X alpestris Nutrition 0.000 description 1
- 235000018212 Betula X uliginosa Nutrition 0.000 description 1
- 102100035687 Bile salt-activated lipase Human genes 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- 101100352919 Caenorhabditis elegans ppm-2 gene Proteins 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 1
- 238000011537 Coomassie blue staining Methods 0.000 description 1
- 241000186216 Corynebacterium Species 0.000 description 1
- 229920001425 Diethylaminoethyl cellulose Polymers 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 241000283073 Equus caballus Species 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- RTVRUWIBAVHRQX-PMEZUWKYSA-N Fucosyllactose Chemical compound C([C@H]1O[C@@H]([C@H]([C@@H](O[C@@H]2[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O2)O)[C@@H]1O)O)OC)O[C@H]1OC[C@@H](O)[C@H](O)[C@@H]1O RTVRUWIBAVHRQX-PMEZUWKYSA-N 0.000 description 1
- 206010017533 Fungal infection Diseases 0.000 description 1
- 102000005744 Glycoside Hydrolases Human genes 0.000 description 1
- 108010031186 Glycoside Hydrolases Proteins 0.000 description 1
- 102000006771 Gonadotropins Human genes 0.000 description 1
- 108010086677 Gonadotropins Proteins 0.000 description 1
- 206010061598 Immunodeficiency Diseases 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- 102000010445 Lactoferrin Human genes 0.000 description 1
- 108010063045 Lactoferrin Proteins 0.000 description 1
- 108010023244 Lactoperoxidase Proteins 0.000 description 1
- 102000045576 Lactoperoxidases Human genes 0.000 description 1
- 108090001090 Lectins Proteins 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 241000699660 Mus musculus Species 0.000 description 1
- 101100121079 Mus musculus Gal gene Proteins 0.000 description 1
- 208000031888 Mycoses Diseases 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 101710202061 N-acetyltransferase Proteins 0.000 description 1
- 241000588660 Neisseria polysaccharea Species 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 108010058846 Ovalbumin Proteins 0.000 description 1
- 239000002033 PVDF binder Substances 0.000 description 1
- 241001337451 Polyblastus cancer Species 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- 241000185994 Pseudarthrobacter oxydans Species 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 241000242678 Schistosoma Species 0.000 description 1
- 241000187180 Streptomyces sp. Species 0.000 description 1
- LFTYTUAZOPRMMI-CFRASDGPSA-N UDP-N-acetyl-alpha-D-glucosamine Chemical compound O1[C@H](CO)[C@@H](O)[C@H](O)[C@@H](NC(=O)C)[C@H]1OP(O)(=O)OP(O)(=O)OC[C@@H]1[C@@H](O)[C@@H](O)[C@H](N2C(NC(=O)C=C2)=O)O1 LFTYTUAZOPRMMI-CFRASDGPSA-N 0.000 description 1
- HSCJRCZFDFQWRP-ABVWGUQPSA-N UDP-alpha-D-galactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1OP(O)(=O)OP(O)(=O)OC[C@@H]1[C@@H](O)[C@@H](O)[C@H](N2C(NC(=O)C=C2)=O)O1 HSCJRCZFDFQWRP-ABVWGUQPSA-N 0.000 description 1
- LFTYTUAZOPRMMI-UHFFFAOYSA-N UNPD164450 Natural products O1C(CO)C(O)C(O)C(NC(=O)C)C1OP(O)(=O)OP(O)(=O)OCC1C(O)C(O)C(N2C(NC(=O)C=C2)=O)O1 LFTYTUAZOPRMMI-UHFFFAOYSA-N 0.000 description 1
- 240000003864 Ulex europaeus Species 0.000 description 1
- 235000010730 Ulex europaeus Nutrition 0.000 description 1
- HSCJRCZFDFQWRP-UHFFFAOYSA-N Uridindiphosphoglukose Natural products OC1C(O)C(O)C(CO)OC1OP(O)(=O)OP(O)(=O)OCC1C(O)C(O)C(N2C(NC(=O)C=C2)=O)O1 HSCJRCZFDFQWRP-UHFFFAOYSA-N 0.000 description 1
- 208000036142 Viral infection Diseases 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 238000005349 anion exchange Methods 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 239000012298 atmosphere Substances 0.000 description 1
- 208000022362 bacterial infectious disease Diseases 0.000 description 1
- 244000052616 bacterial pathogen Species 0.000 description 1
- 108010087173 bile salt-stimulated lipase Proteins 0.000 description 1
- 238000001574 biopsy Methods 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 210000000481 breast Anatomy 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 230000021164 cell adhesion Effects 0.000 description 1
- 230000030570 cellular localization Effects 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 230000004186 co-expression Effects 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 238000002425 crystallisation Methods 0.000 description 1
- 230000008025 crystallization Effects 0.000 description 1
- 239000008367 deionised water Substances 0.000 description 1
- 229910021641 deionized water Inorganic materials 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 235000015872 dietary supplement Nutrition 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 1
- 210000003743 erythrocyte Anatomy 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 230000008020 evaporation Effects 0.000 description 1
- 238000002270 exclusion chromatography Methods 0.000 description 1
- 239000003925 fat Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 108010001671 galactoside 3-fucosyltransferase Proteins 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 210000004602 germ cell Anatomy 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 235000020251 goat milk Nutrition 0.000 description 1
- 210000002288 golgi apparatus Anatomy 0.000 description 1
- 239000002622 gonadotropin Substances 0.000 description 1
- 210000002216 heart Anatomy 0.000 description 1
- 229930195733 hydrocarbon Natural products 0.000 description 1
- 150000002430 hydrocarbons Chemical class 0.000 description 1
- MHAJPDPJQMAIIY-UHFFFAOYSA-N hydrogen peroxide Substances OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 238000002513 implantation Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 230000004054 inflammatory process Effects 0.000 description 1
- 210000004020 intracellular membrane Anatomy 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 210000003734 kidney Anatomy 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
- 238000002372 labelling Methods 0.000 description 1
- 235000021242 lactoferrin Nutrition 0.000 description 1
- 229940078795 lactoferrin Drugs 0.000 description 1
- 229940057428 lactoperoxidase Drugs 0.000 description 1
- 239000002523 lectin Substances 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 239000012160 loading buffer Substances 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 230000013011 mating Effects 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 229940092253 ovalbumin Drugs 0.000 description 1
- 102000013415 peroxidase activity proteins Human genes 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 239000008177 pharmaceutical agent Substances 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 210000004739 secretory vesicle Anatomy 0.000 description 1
- 210000000582 semen Anatomy 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 239000012192 staining solution Substances 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 239000012086 standard solution Substances 0.000 description 1
- 208000002254 stillbirth Diseases 0.000 description 1
- 231100000537 stillbirth Toxicity 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 230000001360 synchronised effect Effects 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 150000004044 tetrasaccharides Chemical class 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 238000012795 verification Methods 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 238000002689 xenotransplantation Methods 0.000 description 1
- 235000021241 α-lactalbumin Nutrition 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
- 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
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/85—Vectors or expression systems specially adapted for eukaryotic hosts for animal cells
- C12N15/8509—Vectors or expression systems specially adapted for eukaryotic hosts for animal cells for producing genetically modified animals, e.g. transgenic
-
- 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
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
- C12N5/10—Cells modified by introduction of foreign genetic material
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K67/00—Rearing or breeding animals, not otherwise provided for; New or modified breeds of animals
- A01K67/027—New or modified breeds of vertebrates
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K67/00—Rearing or breeding animals, not otherwise provided for; New or modified breeds of animals
- A01K67/027—New or modified breeds of vertebrates
- A01K67/0275—Genetically modified vertebrates, e.g. transgenic
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
- A23C9/00—Milk preparations; Milk powder or milk powder preparations
- A23C9/20—Dietetic milk products not covered by groups A23C9/12 - A23C9/18
-
- 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
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/52—Genes encoding for enzymes or proenzymes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/1048—Glycosyltransferases (2.4)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/1048—Glycosyltransferases (2.4)
- C12N9/1051—Hexosyltransferases (2.4.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/1048—Glycosyltransferases (2.4)
- C12N9/1077—Pentosyltransferases (2.4.2)
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2217/00—Genetically modified animals
- A01K2217/05—Animals comprising random inserted nucleic acids (transgenic)
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2227/00—Animals characterised by species
- A01K2227/10—Mammal
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2227/00—Animals characterised by species
- A01K2227/10—Mammal
- A01K2227/105—Murine
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2227/00—Animals characterised by species
- A01K2227/10—Mammal
- A01K2227/107—Rabbit
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2267/00—Animals characterised by purpose
- A01K2267/01—Animal expressing industrially exogenous proteins
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- Chemical & Material Sciences (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Organic Chemistry (AREA)
- Wood Science & Technology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Biochemistry (AREA)
- Environmental Sciences (AREA)
- Medicinal Chemistry (AREA)
- Veterinary Medicine (AREA)
- Animal Husbandry (AREA)
- Physics & Mathematics (AREA)
- Animal Behavior & Ethology (AREA)
- Biophysics (AREA)
- Biodiversity & Conservation Biology (AREA)
- Plant Pathology (AREA)
- Nutrition Science (AREA)
- Food Science & Technology (AREA)
- Polymers & Plastics (AREA)
- Cell Biology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Enzymes And Modification Thereof (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Dairy Products (AREA)
- Fodder In General (AREA)
- Saccharide Compounds (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US08/925,834 US6204431B1 (en) | 1994-03-09 | 1997-09-05 | Transgenic non-human mammals expressing heterologous glycosyltransferase DNA sequences produce oligosaccharides and glycoproteins in their milk |
| PCT/US1998/018383 WO1999011773A1 (en) | 1997-09-05 | 1998-09-04 | Transgenic mammals which produce oligosaccharides in their milk |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| SK3042000A3 true SK3042000A3 (en) | 2000-09-12 |
Family
ID=25452320
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| SK304-2000A SK3042000A3 (en) | 1997-09-05 | 1998-09-04 | Transgenic mammals which produce oligosaccharides in their milk |
Country Status (20)
| Country | Link |
|---|---|
| US (1) | US6204431B1 (es) |
| EP (1) | EP1007651A1 (es) |
| JP (1) | JP2001520001A (es) |
| KR (1) | KR20010023645A (es) |
| CN (1) | CN1273602A (es) |
| AR (1) | AR017515A1 (es) |
| AU (1) | AU9220398A (es) |
| BG (1) | BG104236A (es) |
| BR (1) | BR9811733A (es) |
| CA (1) | CA2302777A1 (es) |
| CO (1) | CO4930313A1 (es) |
| HU (1) | HUP0004709A2 (es) |
| IL (1) | IL133992A0 (es) |
| MX (1) | MXPA00002266A (es) |
| NO (1) | NO20001105L (es) |
| PL (1) | PL339132A1 (es) |
| SK (1) | SK3042000A3 (es) |
| TR (1) | TR200000500T2 (es) |
| WO (1) | WO1999011773A1 (es) |
| ZA (1) | ZA987504B (es) |
Families Citing this family (52)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20030129745A1 (en) | 1999-10-28 | 2003-07-10 | Robl James M. | Gynogenetic or androgenetic production of pluripotent cells and cell lines, and use thereof to produce differentiated cells and tissues |
| US7074983B2 (en) | 1999-11-19 | 2006-07-11 | Kirin Beer Kabushiki Kaisha | Transgenic bovine comprising human immunoglobulin loci and producing human immunoglobulin |
| WO2001035735A1 (en) * | 1999-11-19 | 2001-05-25 | Hematech, Llc | Production of ungulates, preferably bovines that produce human immunoglobulins |
| US7820878B2 (en) * | 1999-11-19 | 2010-10-26 | Kyowa Hakko Kirin Co., Ltd. | Production of ungulates, preferably bovines that produce human immunoglobulins |
| US7414170B2 (en) * | 1999-11-19 | 2008-08-19 | Kirin Beer Kabushiki Kaisha | Transgenic bovines capable of human antibody production |
| US7449308B2 (en) * | 2000-06-28 | 2008-11-11 | Glycofi, Inc. | Combinatorial DNA library for producing modified N-glycans in lower eukaryotes |
| DK1522590T3 (da) | 2000-06-28 | 2009-12-21 | Glycofi Inc | Fremgangsmåde til fremstilling af modificerede glykoproteiner |
| US7598055B2 (en) * | 2000-06-28 | 2009-10-06 | Glycofi, Inc. | N-acetylglucosaminyltransferase III expression in lower eukaryotes |
| US7863020B2 (en) * | 2000-06-28 | 2011-01-04 | Glycofi, Inc. | Production of sialylated N-glycans in lower eukaryotes |
| US8697394B2 (en) * | 2000-06-28 | 2014-04-15 | Glycofi, Inc. | Production of modified glycoproteins having multiple antennary structures |
| US7625756B2 (en) | 2000-06-28 | 2009-12-01 | GycoFi, Inc. | Expression of class 2 mannosidase and class III mannosidase in lower eukaryotic cells |
| US6921665B2 (en) * | 2000-11-27 | 2005-07-26 | Roslin Institute (Edinburgh) | Selective antibody targeting of undifferentiated stem cells |
| US6576464B2 (en) * | 2000-11-27 | 2003-06-10 | Geron Corporation | Methods for providing differentiated stem cells |
| US20060253913A1 (en) * | 2001-12-21 | 2006-11-09 | Yue-Jin Huang | Production of hSA-linked butyrylcholinesterases in transgenic mammals |
| WO2003054182A2 (en) * | 2001-12-21 | 2003-07-03 | Nexia Biotechnologies, Inc. | Production of butyrylcholinesterases in transgenic mammals |
| US7169548B2 (en) | 2002-09-13 | 2007-01-30 | Xy, Inc. | Sperm cell processing and preservation systems |
| RU2384059C2 (ru) * | 2002-11-08 | 2010-03-20 | Киова Хакко Кирин Ко., Лтд. | Трансгенные копытные животные, имеющие пониженную активность прионного белка, и их применения |
| US20040231010A1 (en) * | 2003-01-09 | 2004-11-18 | Murray James D. | Lysozyme transgenic ungulates |
| US7332299B2 (en) | 2003-02-20 | 2008-02-19 | Glycofi, Inc. | Endomannosidases in the modification of glycoproteins in eukaryotes |
| US7514593B2 (en) | 2003-05-30 | 2009-04-07 | The University Of North Carolina At Chapel Hill | Animal model for chronic obstructive pulmonary disease and cystic fibrosis |
| US7771978B2 (en) * | 2003-09-22 | 2010-08-10 | Henrik Clausen | β1,4mannosyltransferases |
| CA2548140A1 (en) * | 2003-12-05 | 2005-06-23 | University Of Massachusetts | Oligosaccharide compositions and use thereof in the treatment of infection |
| WO2005080585A1 (en) * | 2004-02-13 | 2005-09-01 | Glycotope Gmbh | Highly active glycoproteins-process conditions and an efficient method for their production |
| WO2005104835A2 (en) * | 2004-04-22 | 2005-11-10 | Kirin Beer Kabushiki Kaisha | Transgenic animals and uses thereof |
| US20060053500A1 (en) * | 2004-05-28 | 2006-03-09 | Univ. of Pittsburgh of the Commonwealth System of Higher Education, Office of Technology Management | Modification of sugar metabolic processes in transgenic cells, tissues and animals |
| JP5502328B2 (ja) * | 2006-02-09 | 2014-05-28 | メディカゴ インコーポレイテッド | 植物体中でのシアル酸の合成 |
| US7663019B2 (en) * | 2006-05-24 | 2010-02-16 | North Carolina State University | Transgenic snakes and methods of making |
| US8124831B2 (en) * | 2006-07-06 | 2012-02-28 | Duke University | Transgenic mice carrying functional single nucleotide polymorphisms in brain-specific tryptophan hydroxylase |
| JP2009545329A (ja) * | 2006-08-04 | 2009-12-24 | ファーマシーネ，インコーポレイテッド | 長い半減期の組換え型ブチリルコリンエステラーゼ |
| CN101855554B (zh) | 2007-09-07 | 2014-05-14 | 儿童医院医学中心 | 分泌者、Lewis和唾液酸化抗原水平作为疾病预测指标的用途 |
| SG185948A1 (en) * | 2007-11-08 | 2012-12-28 | Nestec Sa | Use of oligosaccharides containing n-acetyllactosamine for maturation of immune responses in neonates |
| NZ596099A (en) | 2009-04-13 | 2013-11-29 | Childrens Hosp Medical Center | Milk oligosaccharide compositions and use thereof in treating infection in animals |
| CN106978382A (zh) * | 2009-06-08 | 2017-07-25 | 詹尼温生物技术有限责任公司 | Hmo合成 |
| EP2451462B1 (en) | 2009-07-06 | 2017-09-06 | Children's Hospital Medical Center | Inhibiting inflammation with milk oligosaccharides |
| MY189329A (en) | 2009-07-15 | 2022-02-04 | Nutricia Nv | Mixture of non-digestible oligosaccharides for stimulating the immune system |
| WO2011008087A1 (en) | 2009-07-15 | 2011-01-20 | N.V. Nutricia | Fucosyllactose as breast milk identical non-digestible oligosaccharide with new functional benefit |
| US8729245B2 (en) | 2009-12-21 | 2014-05-20 | Pharmathene, Inc. | Recombinant butyrylcholinesterases and truncates thereof |
| CA2817765A1 (en) * | 2011-01-06 | 2012-07-12 | The Johns Hopkins University | Method of production of recombinant glycoproteins with increased circulatory half-life in mammalian cells |
| PL2722394T3 (pl) | 2011-06-07 | 2018-09-28 | Hero Ag | Otrzymywanie oligosacharydów za pomocą procesu biotechnologicznego |
| NL2007268C2 (en) | 2011-08-16 | 2013-02-19 | Friesland Brands Bv | Nutritional compositions comprising human milk oligosaccharides and uses thereof. |
| CN102839157A (zh) * | 2012-07-12 | 2012-12-26 | 扬州大学 | 稳定共表达hST3GalIV和β1-4GalT1的MDCK细胞系及构建方法和应用 |
| US20140115728A1 (en) | 2012-10-24 | 2014-04-24 | A. Joseph Tector | Double knockout (gt/cmah-ko) pigs, organs and tissues |
| US10034921B2 (en) * | 2013-02-13 | 2018-07-31 | Laboratoire Français Du Fractionnement Et Des Biotechnologies | Proteins with modified glycosylation and methods of production thereof |
| EP3594231A1 (en) | 2013-02-13 | 2020-01-15 | Laboratoire Français du Fractionnement et des Biotechnologies | Highly galactosylated anti-tnf-alpha antibodies and uses thereof |
| WO2014130789A1 (en) | 2013-02-21 | 2014-08-28 | Children's Hospital Medical Center | Use of glycans and glycosyltransferases for diagnosing/monitoring inflammatory bowel disease |
| CN103196725B (zh) * | 2013-03-26 | 2015-07-08 | 上海交通大学 | 制备与富集单个微纳米珠携带单根多聚物分子的方法 |
| US10857167B2 (en) | 2015-04-28 | 2020-12-08 | Children's Hospital Medical Center | Use of oligosaccharide compositions to enhance weight gain |
| WO2019031961A1 (en) | 2017-08-11 | 2019-02-14 | N.V. Nutricia | OLIGOSACCHARIDE OF HUMAN MILK TO IMPROVE PHYSICAL IMMUNE CONDITION |
| CN112399851A (zh) | 2018-07-11 | 2021-02-23 | 俄亥俄大学 | 基于肽的生长激素作用抑制剂及其使用方法 |
| AU2019473345A1 (en) | 2019-11-05 | 2022-05-05 | Versiti Blood Research Institute Foundation, Inc. | A murine model of fetal/neonatal alloimmune thrombocytopenia |
| US11266129B2 (en) | 2019-11-05 | 2022-03-08 | Versiti Blood Research Institute Foundation, Inc. | Murine model of fetal/neonatal alloimmune thrombocytopenia |
| EP4259827A1 (en) * | 2020-12-11 | 2023-10-18 | Ausnutria B.V. | Increased 2'-fl production by goats |
Family Cites Families (24)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4435363A (en) | 1981-07-02 | 1984-03-06 | Exxon Nuclear Company, Inc. | Continuous countercurrent liquid-solids contactor |
| DE3334167A1 (de) | 1983-09-21 | 1985-04-04 | Siemens AG, 1000 Berlin und 8000 München | Halbleiterdiode |
| US5322775A (en) | 1986-06-30 | 1994-06-21 | Pharmaceutical Proteins Ltd. | Peptide production |
| GB8615942D0 (en) | 1986-06-30 | 1986-08-06 | Animal & Food Research Council | Peptide production |
| AU7879987A (en) | 1986-08-28 | 1988-03-24 | Immunex Corp. | Expression of heterologous proteins by transgenic lactating mammals |
| EP0832981A1 (en) | 1987-02-17 | 1998-04-01 | Pharming B.V. | DNA sequences to target proteins to the mammary gland for efficient secretion |
| GB8826446D0 (en) | 1988-11-11 | 1988-12-14 | Agricultural & Food Res | Peptide production |
| US5032519A (en) | 1989-10-24 | 1991-07-16 | The Regents Of The Univ. Of California | Method for producing secretable glycosyltransferases and other Golgi processing enzymes |
| EP0737746A3 (en) | 1989-12-01 | 1996-10-23 | Pharming B.V. | Production of recombinant polypeptides by bovine species and transgenic methods |
| WO1991016449A1 (en) | 1990-04-16 | 1991-10-31 | The Trustees Of The University Of Pennsylvania | Saccharide compositions, methods and apparatus for their synthesis |
| US5612205A (en) | 1990-08-29 | 1997-03-18 | Genpharm International, Incorporated | Homologous recombination in mammalian cells |
| US5198466A (en) | 1990-11-09 | 1993-03-30 | Warner-Lambert Company | Oxysulfonyl urea acat inhibitors |
| US5362480A (en) | 1991-12-31 | 1994-11-08 | Lever Brothers Company, Division Of Conopco, Inc. | Oral hygiene compositions containing amino sugars as antiplaque agents |
| DK8892D0 (da) | 1992-01-23 | 1992-01-23 | Symbicom Ab | Humant proteingen |
| US5401723A (en) | 1992-12-02 | 1995-03-28 | Colgate-Palmolive Company | Glycoconjugate inhibition of Streptococcus pyrogenes adhesion |
| AU6042594A (en) | 1993-02-26 | 1994-09-14 | Thomas Boren | Use of oligosaccharide glycosides as inhibitors of bacterial adherence |
| DK76193D0 (da) | 1993-06-25 | 1993-06-25 | Astra Ab | Kulhydratderivater |
| NZ279676A (en) * | 1994-03-09 | 1998-04-27 | Abbott Lab | Humanized milk produced by non-human transgenic mammal transformed with a heterologous gene coding for human enzyme producing human oligosaccharides and glycoconjugates |
| MX198456B (es) * | 1994-03-09 | 2000-09-05 | Abbott Lab | Animales trangenicos que producen oligosacaridos y glucoconjugados. |
| US5750176A (en) | 1994-03-09 | 1998-05-12 | Abbott Laboratories | Transgenic non-human mammal milk comprising 2'-fucosyl-lactose |
| US5625124A (en) | 1994-07-11 | 1997-04-29 | Washington University | Animal model for helicobacter pylori infection |
| HUP9900058A2 (hu) | 1995-09-29 | 1999-04-28 | Glycim Oy | Polilaktózaminokat tartalmazó szintetikus multivalens sLEX és eljárások az alkalmazására |
| US5874411A (en) | 1995-11-13 | 1999-02-23 | Glycomed Incorporated | Oligosaccharide glycosides having mammalian immunosuppresive and tolerogenic properties |
| WO1997018790A2 (en) | 1995-11-22 | 1997-05-29 | The Research And Development Institute, Inc. | Therapeutic and diagnostic agents for the treatment of microbial infections |
-
1997
- 1997-09-05 US US08/925,834 patent/US6204431B1/en not_active Expired - Fee Related
-
1998
- 1998-08-19 ZA ZA987504A patent/ZA987504B/xx unknown
- 1998-09-04 PL PL98339132A patent/PL339132A1/xx unknown
- 1998-09-04 TR TR2000/00500T patent/TR200000500T2/xx unknown
- 1998-09-04 IL IL13399298A patent/IL133992A0/xx unknown
- 1998-09-04 EP EP98944736A patent/EP1007651A1/en not_active Withdrawn
- 1998-09-04 JP JP2000508784A patent/JP2001520001A/ja active Pending
- 1998-09-04 CN CN98808662A patent/CN1273602A/zh active Pending
- 1998-09-04 KR KR1020007002297A patent/KR20010023645A/ko not_active Application Discontinuation
- 1998-09-04 HU HU0004709A patent/HUP0004709A2/hu unknown
- 1998-09-04 AU AU92203/98A patent/AU9220398A/en not_active Abandoned
- 1998-09-04 CA CA002302777A patent/CA2302777A1/en not_active Abandoned
- 1998-09-04 BR BR9811733-5A patent/BR9811733A/pt not_active IP Right Cessation
- 1998-09-04 SK SK304-2000A patent/SK3042000A3/sk unknown
- 1998-09-04 CO CO98050804A patent/CO4930313A1/es unknown
- 1998-09-04 AR ARP980104420A patent/AR017515A1/es unknown
- 1998-09-04 WO PCT/US1998/018383 patent/WO1999011773A1/en not_active Application Discontinuation
-
2000
- 2000-03-03 MX MXPA00002266 patent/MXPA00002266A/es unknown
- 2000-03-03 NO NO20001105A patent/NO20001105L/no not_active Application Discontinuation
- 2000-03-13 BG BG104236A patent/BG104236A/xx unknown
Also Published As
| Publication number | Publication date |
|---|---|
| NO20001105L (no) | 2000-05-05 |
| JP2001520001A (ja) | 2001-10-30 |
| NO20001105D0 (no) | 2000-03-03 |
| HUP0004709A2 (hu) | 2001-04-28 |
| US6204431B1 (en) | 2001-03-20 |
| WO1999011773A1 (en) | 1999-03-11 |
| KR20010023645A (ko) | 2001-03-26 |
| MXPA00002266A (es) | 2000-10-01 |
| CN1273602A (zh) | 2000-11-15 |
| BG104236A (en) | 2000-12-29 |
| AR017515A1 (es) | 2001-09-12 |
| PL339132A1 (en) | 2000-12-04 |
| CO4930313A1 (es) | 2000-06-27 |
| EP1007651A1 (en) | 2000-06-14 |
| TR200000500T2 (tr) | 2000-12-21 |
| BR9811733A (pt) | 2000-09-05 |
| CA2302777A1 (en) | 1999-03-11 |
| ZA987504B (en) | 1999-03-15 |
| IL133992A0 (en) | 2001-04-30 |
| AU9220398A (en) | 1999-03-22 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| SK3042000A3 (en) | Transgenic mammals which produce oligosaccharides in their milk | |
| US5891698A (en) | Oligosaccharides and glycoproteins produced in milk of transgenic non-human mammals | |
| US5700671A (en) | Methods of making transgenic animals producing oligosaccharides and glycoproteins | |
| US5750176A (en) | Transgenic non-human mammal milk comprising 2'-fucosyl-lactose | |
| MXPA96003892A (es) | Metodo para producir animales transgenicos que producen oligosacaridos y glucoproteinas | |
| US6331658B1 (en) | Genetically engineered mammals for use as organ donors | |
| MXPA96003890A (es) | Leche de mamiferos transgenicos no humanosconteniendo 2'fucosil-lactosa | |
| US10034921B2 (en) | Proteins with modified glycosylation and methods of production thereof | |
| Park et al. | Recombinant human erythropoietin produced in milk of transgenic pigs | |
| US7166278B2 (en) | Modified organs and cells for xenotransplantation | |
| WO1999008511A1 (en) | Methods for producing sialyloligosaccharides in a dairy source | |
| Meade et al. | Expression of recombinant proteins in the milk of transgenic animals | |
| CZ2000803A3 (cs) | Transgenní savci produkující oligosacharidy ve svém mléku | |
| MXPA96003893A (es) | Leche humanizada |