IL88621A - And המקודד גלוקוצרברוסידזה ותהליך להכנתו - Google Patents

And המקודד גלוקוצרברוסידזה ותהליך להכנתו

Info

Publication number: IL88621A
Authority: IL; Israel
Prior art keywords: leu; ala; ser; gly; pro
Prior art date: 1987-12-23

Application number

IL8862188A

Other languages

English (en)

Other versions

IL88621A0 (en

Original Assignee

Us Healt

Priority date (The priority date 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 date listed.)

1987-12-23

Filing date

1988-12-07

Publication date

1995-10-31

Family has litigation

First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=22479076&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=IL88621(A) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.

1988-12-07 Application filed by Us Healt filed Critical Us Healt

1989-07-31 Publication of IL88621A0 publication Critical patent/IL88621A0/xx

1995-10-31 Publication of IL88621A publication Critical patent/IL88621A/he

Links

238000004519 manufacturing process Methods 0.000 title description 3
108010017544 Glucosylceramidase Proteins 0.000 claims description 71
241000701447 unidentified baculovirus Species 0.000 claims description 29
239000002299 complementary DNA Substances 0.000 claims description 25
241000256251 Spodoptera frugiperda Species 0.000 claims description 14
238000000034 method Methods 0.000 claims description 14
241000238631 Hexapoda Species 0.000 claims description 13
239000013598 vector Substances 0.000 claims description 12
108091026890 Coding region Proteins 0.000 claims description 9
239000013612 plasmid Substances 0.000 claims description 9
150000001413 amino acids Chemical group 0.000 claims description 8
239000013604 expression vector Substances 0.000 claims description 8
239000002773 nucleotide Substances 0.000 claims description 7
125000003729 nucleotide group Chemical group 0.000 claims description 7
108091033319 polynucleotide Proteins 0.000 claims description 7
239000002157 polynucleotide Substances 0.000 claims description 7
102000040430 polynucleotide Human genes 0.000 claims description 7
101710182846 Polyhedrin Proteins 0.000 claims description 5
HHRAXZAYZFFRAM-CIUDSAMLSA-N Ala-Leu-Asn Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(O)=O HHRAXZAYZFFRAM-CIUDSAMLSA-N 0.000 claims description 4
BPANDPNDMJHFEV-CIUDSAMLSA-N Leu-Asp-Ala Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C)C(O)=O BPANDPNDMJHFEV-CIUDSAMLSA-N 0.000 claims description 4
NMELOOXSGDRBRU-YUMQZZPRSA-N Pro-Glu-Gly Chemical compound OC(=O)CNC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H]1CCCN1 NMELOOXSGDRBRU-YUMQZZPRSA-N 0.000 claims description 4
WGDYNRCOQRERLZ-KKUMJFAQSA-N Ser-Lys-Phe Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)N WGDYNRCOQRERLZ-KKUMJFAQSA-N 0.000 claims description 4
XBGGUPMXALFZOT-UHFFFAOYSA-N glycyl-L-tyrosine hemihydrate Natural products NCC(=O)NC(C(O)=O)CC1=CC=C(O)C=C1 XBGGUPMXALFZOT-UHFFFAOYSA-N 0.000 claims description 4
108010087823 glycyltyrosine Proteins 0.000 claims description 4
108010051242 phenylalanylserine Proteins 0.000 claims description 4
108010070643 prolylglutamic acid Proteins 0.000 claims description 4
230000001225 therapeutic effect Effects 0.000 claims description 4
UHPAZODVFFYEEL-QWRGUYRKSA-N Gly-Leu-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)CN UHPAZODVFFYEEL-QWRGUYRKSA-N 0.000 claims description 3
239000008194 pharmaceutical composition Substances 0.000 claims description 3
230000008569 process Effects 0.000 claims description 3
230000022532 regulation of transcription, DNA-dependent Effects 0.000 claims description 3
108010061238 threonyl-glycine Proteins 0.000 claims description 3
PIDRBUDUWHBYSR-UHFFFAOYSA-N 1-[2-[[2-[(2-amino-4-methylpentanoyl)amino]-4-methylpentanoyl]amino]-4-methylpentanoyl]pyrrolidine-2-carboxylic acid Chemical compound CC(C)CC(N)C(=O)NC(CC(C)C)C(=O)NC(CC(C)C)C(=O)N1CCCC1C(O)=O PIDRBUDUWHBYSR-UHFFFAOYSA-N 0.000 claims description 2
SSSROGPPPVTHLX-FXQIFTODSA-N Ala-Arg-Asp Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(O)=O SSSROGPPPVTHLX-FXQIFTODSA-N 0.000 claims description 2
HGRBNYQIMKTUNT-XVYDVKMFSA-N Ala-Asn-His Chemical compound C[C@@H](C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)N HGRBNYQIMKTUNT-XVYDVKMFSA-N 0.000 claims description 2
MNZHHDPWDWQJCQ-YUMQZZPRSA-N Ala-Leu-Gly Chemical compound C[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)NCC(O)=O MNZHHDPWDWQJCQ-YUMQZZPRSA-N 0.000 claims description 2
OPZJWMJPCNNZNT-DCAQKATOSA-N Ala-Leu-Met Chemical compound C[C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)O)N OPZJWMJPCNNZNT-DCAQKATOSA-N 0.000 claims description 2
SOBIAADAMRHGKH-CIUDSAMLSA-N Ala-Leu-Ser Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(O)=O SOBIAADAMRHGKH-CIUDSAMLSA-N 0.000 claims description 2
MDNAVFBZPROEHO-UHFFFAOYSA-N Ala-Lys-Val Natural products CC(C)C(C(O)=O)NC(=O)C(NC(=O)C(C)N)CCCCN MDNAVFBZPROEHO-UHFFFAOYSA-N 0.000 claims description 2
IPZQNYYAYVRKKK-FXQIFTODSA-N Ala-Pro-Ala Chemical compound C[C@H](N)C(=O)N1CCC[C@H]1C(=O)N[C@@H](C)C(O)=O IPZQNYYAYVRKKK-FXQIFTODSA-N 0.000 claims description 2
NZGRHTKZFSVPAN-BIIVOSGPSA-N Ala-Ser-Pro Chemical compound C[C@@H](C(=O)N[C@@H](CO)C(=O)N1CCC[C@@H]1C(=O)O)N NZGRHTKZFSVPAN-BIIVOSGPSA-N 0.000 claims description 2
VHAQSYHSDKERBS-XPUUQOCRSA-N Ala-Val-Gly Chemical compound C[C@H](N)C(=O)N[C@@H](C(C)C)C(=O)NCC(O)=O VHAQSYHSDKERBS-XPUUQOCRSA-N 0.000 claims description 2
CLOMBHBBUKAUBP-LSJOCFKGSA-N Ala-Val-His Chemical compound C[C@@H](C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)N CLOMBHBBUKAUBP-LSJOCFKGSA-N 0.000 claims description 2
REWSWYIDQIELBE-FXQIFTODSA-N Ala-Val-Ser Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CO)C(O)=O REWSWYIDQIELBE-FXQIFTODSA-N 0.000 claims description 2
TTXYKSADPSNOIF-IHRRRGAJSA-N Arg-Asp-Phe Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O TTXYKSADPSNOIF-IHRRRGAJSA-N 0.000 claims description 2
SYAUZLVLXCDRSH-IUCAKERBSA-N Arg-Gly-Met Chemical compound CSCC[C@@H](C(=O)O)NC(=O)CNC(=O)[C@H](CCCN=C(N)N)N SYAUZLVLXCDRSH-IUCAKERBSA-N 0.000 claims description 2
VIINVRPKMUZYOI-DCAQKATOSA-N Arg-Met-Glu Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(O)=O)C(O)=O VIINVRPKMUZYOI-DCAQKATOSA-N 0.000 claims description 2
VUGWHBXPMAHEGZ-SRVKXCTJSA-N Arg-Pro-Val Chemical compound CC(C)[C@@H](C(O)=O)NC(=O)[C@@H]1CCCN1C(=O)[C@@H](N)CCCN=C(N)N VUGWHBXPMAHEGZ-SRVKXCTJSA-N 0.000 claims description 2
FRBAHXABMQXSJQ-FXQIFTODSA-N Arg-Ser-Ser Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(O)=O FRBAHXABMQXSJQ-FXQIFTODSA-N 0.000 claims description 2
OGZBJJLRKQZRHL-KJEVXHAQSA-N Arg-Thr-Tyr Chemical compound NC(N)=NCCC[C@H](N)C(=O)N[C@@H]([C@H](O)C)C(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 OGZBJJLRKQZRHL-KJEVXHAQSA-N 0.000 claims description 2
PJOPLXOCKACMLK-KKUMJFAQSA-N Arg-Tyr-Glu Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CCC(O)=O)C(O)=O PJOPLXOCKACMLK-KKUMJFAQSA-N 0.000 claims description 2
LFWOQHSQNCKXRU-UFYCRDLUSA-N Arg-Tyr-Phe Chemical compound C([C@H](NC(=O)[C@H](CCCN=C(N)N)N)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)C1=CC=C(O)C=C1 LFWOQHSQNCKXRU-UFYCRDLUSA-N 0.000 claims description 2
VYZBPPBKFCHCIS-WPRPVWTQSA-N Arg-Val-Gly Chemical compound OC(=O)CNC(=O)[C@H](C(C)C)NC(=O)[C@@H](N)CCCN=C(N)N VYZBPPBKFCHCIS-WPRPVWTQSA-N 0.000 claims description 2
SUMJNGAMIQSNGX-TUAOUCFPSA-N Arg-Val-Pro Chemical compound CC(C)[C@H](NC(=O)[C@@H](N)CCCNC(N)=N)C(=O)N1CCC[C@@H]1C(O)=O SUMJNGAMIQSNGX-TUAOUCFPSA-N 0.000 claims description 2
CTQIOCMSIJATNX-WHFBIAKZSA-N Asn-Gly-Ala Chemical compound [H]N[C@@H](CC(N)=O)C(=O)NCC(=O)N[C@@H](C)C(O)=O CTQIOCMSIJATNX-WHFBIAKZSA-N 0.000 claims description 2
GLWFAWNYGWBMOC-SRVKXCTJSA-N Asn-Leu-Leu Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(O)=O GLWFAWNYGWBMOC-SRVKXCTJSA-N 0.000 claims description 2
UYCPJVYQYARFGB-YDHLFZDLSA-N Asn-Phe-Val Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](C(C)C)C(O)=O UYCPJVYQYARFGB-YDHLFZDLSA-N 0.000 claims description 2
HPNDKUOLNRVRAY-BIIVOSGPSA-N Asn-Ser-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CO)NC(=O)[C@H](CC(=O)N)N)C(=O)O HPNDKUOLNRVRAY-BIIVOSGPSA-N 0.000 claims description 2
HNXWVVHIGTZTBO-LKXGYXEUSA-N Asn-Ser-Thr Chemical compound C[C@@H](O)[C@@H](C(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O HNXWVVHIGTZTBO-LKXGYXEUSA-N 0.000 claims description 2
XIDSGDJNUJRUHE-VEVYYDQMSA-N Asn-Thr-Met Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCSC)C(O)=O XIDSGDJNUJRUHE-VEVYYDQMSA-N 0.000 claims description 2
LTCKTLYKRMCFOC-KKUMJFAQSA-N Asp-Phe-Leu Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CC(C)C)C(O)=O LTCKTLYKRMCFOC-KKUMJFAQSA-N 0.000 claims description 2
BKOIIURTQAJHAT-GUBZILKMSA-N Asp-Pro-Pro Chemical compound OC(=O)C[C@H](N)C(=O)N1CCC[C@H]1C(=O)N1[C@H](C(O)=O)CCC1 BKOIIURTQAJHAT-GUBZILKMSA-N 0.000 claims description 2
ZQFRDAZBTSFGGW-SRVKXCTJSA-N Asp-Ser-Phe Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O ZQFRDAZBTSFGGW-SRVKXCTJSA-N 0.000 claims description 2
NAAAPCLFJPURAM-HJGDQZAQSA-N Asp-Thr-Lys Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CCCCN)C(=O)O)NC(=O)[C@H](CC(=O)O)N)O NAAAPCLFJPURAM-HJGDQZAQSA-N 0.000 claims description 2
PDIYGFYAMZZFCW-JIOCBJNQSA-N Asp-Thr-Pro Chemical compound C[C@H]([C@@H](C(=O)N1CCC[C@@H]1C(=O)O)NC(=O)[C@H](CC(=O)O)N)O PDIYGFYAMZZFCW-JIOCBJNQSA-N 0.000 claims description 2
HRJLVSQKBLZHSR-ZLUOBGJFSA-N Cys-Asn-Ala Chemical compound [H]N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(O)=O HRJLVSQKBLZHSR-ZLUOBGJFSA-N 0.000 claims description 2
IZUNQDRIAOLWCN-YUMQZZPRSA-N Cys-Leu-Gly Chemical compound CC(C)C[C@@H](C(=O)NCC(=O)O)NC(=O)[C@H](CS)N IZUNQDRIAOLWCN-YUMQZZPRSA-N 0.000 claims description 2
AZDQAZRURQMSQD-XPUUQOCRSA-N Cys-Val-Gly Chemical compound [H]N[C@@H](CS)C(=O)N[C@@H](C(C)C)C(=O)NCC(O)=O AZDQAZRURQMSQD-XPUUQOCRSA-N 0.000 claims description 2
YYOBUPFZLKQUAX-FXQIFTODSA-N Glu-Asn-Glu Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O YYOBUPFZLKQUAX-FXQIFTODSA-N 0.000 claims description 2
SJPMNHCEWPTRBR-BQBZGAKWSA-N Glu-Glu-Gly Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(O)=O SJPMNHCEWPTRBR-BQBZGAKWSA-N 0.000 claims description 2
PUUYVMYCMIWHFE-BQBZGAKWSA-N Gly-Ala-Arg Chemical compound NCC(=O)N[C@@H](C)C(=O)N[C@H](C(O)=O)CCCN=C(N)N PUUYVMYCMIWHFE-BQBZGAKWSA-N 0.000 claims description 2
PHONXOACARQMPM-BQBZGAKWSA-N Gly-Ala-Met Chemical compound [H]NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCSC)C(O)=O PHONXOACARQMPM-BQBZGAKWSA-N 0.000 claims description 2
HPAIKDPJURGQLN-KBPBESRZSA-N Gly-His-Phe Chemical compound C([C@H](NC(=O)CN)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)C1=CNC=N1 HPAIKDPJURGQLN-KBPBESRZSA-N 0.000 claims description 2
IGOYNRWLWHWAQO-JTQLQIEISA-N Gly-Phe-Gly Chemical compound OC(=O)CNC(=O)[C@@H](NC(=O)CN)CC1=CC=CC=C1 IGOYNRWLWHWAQO-JTQLQIEISA-N 0.000 claims description 2
SCJJPCQUJYPHRZ-BQBZGAKWSA-N Gly-Pro-Asn Chemical compound NCC(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(N)=O)C(O)=O SCJJPCQUJYPHRZ-BQBZGAKWSA-N 0.000 claims description 2
IRJWAYCXIYUHQE-WHFBIAKZSA-N Gly-Ser-Ala Chemical compound OC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)CN IRJWAYCXIYUHQE-WHFBIAKZSA-N 0.000 claims description 2
XBGGUPMXALFZOT-VIFPVBQESA-N Gly-Tyr Chemical compound NCC(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 XBGGUPMXALFZOT-VIFPVBQESA-N 0.000 claims description 2
JBCLFWXMTIKCCB-UHFFFAOYSA-N H-Gly-Phe-OH Natural products NCC(=O)NC(C(O)=O)CC1=CC=CC=C1 JBCLFWXMTIKCCB-UHFFFAOYSA-N 0.000 claims description 2
TVQGUFGDVODUIF-LSJOCFKGSA-N His-Arg-Ala Chemical compound C[C@@H](C(=O)O)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC1=CN=CN1)N TVQGUFGDVODUIF-LSJOCFKGSA-N 0.000 claims description 2
CTJHHEQNUNIYNN-SRVKXCTJSA-N His-His-Asn Chemical compound [H]N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC(N)=O)C(O)=O CTJHHEQNUNIYNN-SRVKXCTJSA-N 0.000 claims description 2
UXSATKFPUVZVDK-KKUMJFAQSA-N His-Lys-Leu Chemical compound CC(C)C[C@@H](C(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC1=CN=CN1)N UXSATKFPUVZVDK-KKUMJFAQSA-N 0.000 claims description 2
BZAQOPHNBFOOJS-DCAQKATOSA-N His-Pro-Asp Chemical compound [H]N[C@@H](CC1=CNC=N1)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(O)=O)C(O)=O BZAQOPHNBFOOJS-DCAQKATOSA-N 0.000 claims description 2
DEMIXZCKUXVEBO-BWAGICSOSA-N His-Thr-Tyr Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CC1=CC=C(C=C1)O)C(=O)O)NC(=O)[C@H](CC2=CN=CN2)N)O DEMIXZCKUXVEBO-BWAGICSOSA-N 0.000 claims description 2
UIRUVUUGUYCMBY-KCTSRDHCSA-N His-Trp-Ala Chemical compound C[C@@H](C(=O)O)NC(=O)[C@H](CC1=CNC2=CC=CC=C21)NC(=O)[C@H](CC3=CN=CN3)N UIRUVUUGUYCMBY-KCTSRDHCSA-N 0.000 claims description 2
QLROSWPKSBORFJ-BQBZGAKWSA-N L-Prolyl-L-glutamic acid Chemical compound OC(=O)CC[C@@H](C(O)=O)NC(=O)[C@@H]1CCCN1 QLROSWPKSBORFJ-BQBZGAKWSA-N 0.000 claims description 2
WGNOPSQMIQERPK-UHFFFAOYSA-N Leu-Asn-Pro Natural products CC(C)CC(N)C(=O)NC(CC(=O)N)C(=O)N1CCCC1C(=O)O WGNOPSQMIQERPK-UHFFFAOYSA-N 0.000 claims description 2
DLFAACQHIRSQGG-CIUDSAMLSA-N Leu-Asp-Asp Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(O)=O)C(O)=O DLFAACQHIRSQGG-CIUDSAMLSA-N 0.000 claims description 2
KGCLIYGPQXUNLO-IUCAKERBSA-N Leu-Gly-Glu Chemical compound CC(C)C[C@H](N)C(=O)NCC(=O)N[C@H](C(O)=O)CCC(O)=O KGCLIYGPQXUNLO-IUCAKERBSA-N 0.000 claims description 2
YFBBUHJJUXXZOF-UWVGGRQHSA-N Leu-Gly-Pro Chemical compound CC(C)C[C@H](N)C(=O)NCC(=O)N1CCC[C@H]1C(O)=O YFBBUHJJUXXZOF-UWVGGRQHSA-N 0.000 claims description 2
BTNXKBVLWJBTNR-SRVKXCTJSA-N Leu-His-Asn Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CC(N)=O)C(O)=O BTNXKBVLWJBTNR-SRVKXCTJSA-N 0.000 claims description 2
PPQRKXHCLYCBSP-IHRRRGAJSA-N Leu-Leu-Met Chemical compound CC(C)C[C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)O)N PPQRKXHCLYCBSP-IHRRRGAJSA-N 0.000 claims description 2
LVTJJOJKDCVZGP-QWRGUYRKSA-N Leu-Lys-Gly Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)NCC(O)=O LVTJJOJKDCVZGP-QWRGUYRKSA-N 0.000 claims description 2
VCHVSKNMTXWIIP-SRVKXCTJSA-N Leu-Lys-Ser Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CO)C(O)=O VCHVSKNMTXWIIP-SRVKXCTJSA-N 0.000 claims description 2
OVZLLFONXILPDZ-VOAKCMCISA-N Leu-Lys-Thr Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O OVZLLFONXILPDZ-VOAKCMCISA-N 0.000 claims description 2
ZDBMWELMUCLUPL-QEJZJMRPSA-N Leu-Phe-Ala Chemical compound CC(C)C[C@H](N)C(=O)N[C@H](C(=O)N[C@@H](C)C(O)=O)CC1=CC=CC=C1 ZDBMWELMUCLUPL-QEJZJMRPSA-N 0.000 claims description 2
UHNQRAFSEBGZFZ-YESZJQIVSA-N Leu-Phe-Pro Chemical compound CC(C)C[C@@H](C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N2CCC[C@@H]2C(=O)O)N UHNQRAFSEBGZFZ-YESZJQIVSA-N 0.000 claims description 2
GOFJOGXGMPHOGL-DCAQKATOSA-N Leu-Ser-Met Chemical compound CSCC[C@@H](C(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(C)C GOFJOGXGMPHOGL-DCAQKATOSA-N 0.000 claims description 2
SBANPBVRHYIMRR-UHFFFAOYSA-N Leu-Ser-Pro Natural products CC(C)CC(N)C(=O)NC(CO)C(=O)N1CCCC1C(O)=O SBANPBVRHYIMRR-UHFFFAOYSA-N 0.000 claims description 2
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Classifications

- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01045—Glucosylceramidase (3.2.1.45), i.e. beta-glucocerebrosidase
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- 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
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides

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Chemical & Material Sciences (AREA)
Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Organic Chemistry (AREA)
Engineering & Computer Science (AREA)
Bioinformatics & Cheminformatics (AREA)
Zoology (AREA)
Wood Science & Technology (AREA)
Genetics & Genomics (AREA)
General Health & Medical Sciences (AREA)
General Engineering & Computer Science (AREA)
Biochemistry (AREA)
Medicinal Chemistry (AREA)
Biotechnology (AREA)
Molecular Biology (AREA)
Biomedical Technology (AREA)
Microbiology (AREA)
Chemical Kinetics & Catalysis (AREA)
Veterinary Medicine (AREA)
Public Health (AREA)
Animal Behavior & Ethology (AREA)
Pharmacology & Pharmacy (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
General Chemical & Material Sciences (AREA)
Obesity (AREA)
Hematology (AREA)
Diabetes (AREA)
Enzymes And Modification Thereof (AREA)

IL8862188A 1987-12-23 1988-12-07 And המקודד גלוקוצרברוסידזה ותהליך להכנתו IL88621A (he)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
US13779687A	1987-12-23	1987-12-23

Publications (2)

Publication Number	Publication Date
IL88621A0 IL88621A0 (en)	1989-07-31
IL88621A true IL88621A (he)	1995-10-31

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ID=22479076

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IL8862188A IL88621A (he)	1987-12-23	1988-12-07	And המקודד גלוקוצרברוסידזה ותהליך להכנתו

Country Status (6)

Country	Link
US (1)	US6074864A (he)
EP (1)	EP0393143A4 (he)
AU (1)	AU2946289A (he)
CA (1)	CA1340829C (he)
IL (1)	IL88621A (he)
WO (1)	WO1989005850A1 (he)

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US4949082A (en) *	1988-07-06	1990-08-14	Nei Canada Limited	High speed display device
DE68926569T2 (de) *	1988-12-23	1996-09-26	Genzyme Corp	Cho-zellen befähigt enzymatisch aktive rekombinante-glukocerebrosidase zu produzieren
EP0448513A3 (en) *	1990-03-21	1991-12-27	Japat Ltd	Process for production of peptidylglycine alpha-hydroxylating monooxygenase and use thereof
DK0675727T3 (da) *	1992-12-10	2002-08-05	Enzon Inc	Glycolipidenzympolymerkonjugater
US20090148906A1 (en) *	1998-09-29	2009-06-11	Shire Human Genetic Therapies, Inc. A Delaware Corporation	Optimized messenger rna
WO2001077307A2 (en) *	2000-04-06	2001-10-18	Exegenics, Inc.	Expression system for efficiently producing clinically effective lysosomal enzymes (glucocerebrosidase)
US7138262B1 (en) *	2000-08-18	2006-11-21	Shire Human Genetic Therapies, Inc.	High mannose proteins and methods of making high mannose proteins
US7740861B2 (en)	2004-06-16	2010-06-22	University Of Massachusetts	Drug delivery product and methods
AU2005284727A1 (en)	2004-09-17	2006-03-23	University Of Massachusetts	Compositions and their uses for lysosomal enzyme deficiencies
US7776377B2 (en) *	2005-03-03	2010-08-17	Green Rabbit, Llc	Non-dairy, non-soy food product and methods of making
ATE526991T1 (de) *	2005-10-24	2011-10-15	Univ Massachusetts	Zusammensetzungen und ihre verwendungen für die gentherapeutische behandlung von knochenerkrankungen
HRP20120994T1 (hr)	2006-02-07	2012-12-31	Shire Human Genetic Therapies, Inc.	Stabilizirana smjesa glukocerebrozidaze
EP2222283A2 (en)	2007-10-29	2010-09-01	University of Massachusetts	Yeast cell wall protein (ycwp) encapsulated multilayered nanoparticles for nucleic acid delivery (sirna)
US20110318322A1 (en) *	2009-01-12	2011-12-29	Nektar Therapeutics	Conjugates of a Lysosomal Enzyme Moiety and a Water Soluble Polymer
NZ713967A (en)	2009-07-28	2017-01-27	Shire Human Genetic Therapies	Compositions and methods for treating gaucher disease
EP2595651B1 (en)	2010-07-19	2017-03-29	Shire Human Genetic Therapies, Inc.	Mannose receptor c type 1 (mrc1) codon optimized cell line and uses thereof
CN104519905A (zh)	2012-03-02	2015-04-15	夏尔人类遗传性治疗公司	用于治疗iii型戈谢病的组合物和方法

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Publication number	Priority date	Publication date	Assignee	Title
US4745051A (en) *	1983-05-27	1988-05-17	The Texas A&M University System	Method for producing a recombinant baculovirus expression vector

1988
- 1988-11-30 WO PCT/US1988/004314 patent/WO1989005850A1/en not_active Ceased
- 1988-11-30 AU AU29462/89A patent/AU2946289A/en not_active Abandoned
- 1988-11-30 EP EP19890901645 patent/EP0393143A4/en not_active Withdrawn
- 1988-12-07 IL IL8862188A patent/IL88621A/he active IP Right Review Request
- 1988-12-20 CA CA000586401A patent/CA1340829C/en not_active Expired - Fee Related
1994
- 1994-01-13 US US08/186,256 patent/US6074864A/en not_active Expired - Fee Related

Also Published As

Publication number	Publication date
IL88621A0 (en)	1989-07-31
WO1989005850A1 (en)	1989-06-29
EP0393143A1 (en)	1990-10-24
CA1340829C (en)	1999-11-23
AU2946289A (en)	1989-07-19
EP0393143A4 (en)	1991-09-11
US6074864A (en)	2000-06-13

Legal Events

Date	Code	Title	Description
1997-03-18	CE	Application withdrawn (oppos. filed against grant of patent)	Free format text: APPLICANT WITHDREW APPLICATION ON 22.5.96
1997-08-14	NP	Permission for amending the patent specification granted (section 66, patents law 1967)
1998-02-22	CB	Opposition filed against grant of patent
1998-09-24	KB	Patent renewed
2003-02-12	KB	Patent renewed
2007-02-12	KB	Patent renewed

Publication	Publication Date	Title
US5879680A (en)	1999-03-09	Cloned DNA for synthesizing unique glucocerebrosidase
US6074864A (en)	2000-06-13	Cloned DNA for synthesizing unique glucocerebrosidase
US5179023A (en)	1993-01-12	Recombinant α-galactosidase a therapy for Fabry disease
RU2009198C1 (ru)	1994-03-15	Фрагмент нуклеиновой кислоты, кодирующий человеческий проаполипопротеин а-1
US6451600B1 (en)	2002-09-17	Enzymatically active recombinant glucocerebrosidase
US5622832A (en)	1997-04-22	Arachidonic acid releasing phospholipase A2 enzyme and methods of use
Martin et al.	1988	Glycosylation and processing of high levels of active human glucocerebrosidase in invertebrate cells using a baculovirus expression vector
JP2936201B2 (ja)	1999-08-23	ヒト第▲ｉｘ▼因子または類似の蛋白質をコードするｄｎａ配列、発現ベクター、形質転換された細胞、第▲ｉｘ▼因子の製造方法および得られた対応する生成物
JPH10503645A (ja)	1998-04-07	バキュロウイルスにより発現される活性カルパイン
JP2002255999A (ja)	2002-09-11	組換えｄｎａ合成システムにおけるヒトプロコラーゲン及びコラーゲンの合成
JP2893481B2 (ja)	1999-05-24	酵素的に活性な組換えグルコセレブロシダーゼ
WO1990011353A1 (en)	1990-10-04	Recombinant alpha-galactosidase, a therapy for fabry disease
AU691929B2 (en)	1998-05-28	Nucleic acid sequence encoding trypsin-like enzyme and process for producing the enzyme
WO1994026908A1 (en)	1994-11-24	Cho cell sialidase by recombinant dna technology
US6323017B1 (en)	2001-11-27	Platelet activating factor acetylhydrolase, and gene thereof
CA1300534C (en)	1992-05-12	Human pancreatic elastase
Coppola et al.	1994	Characterization of glycosylated and catalytically active recombinant human α-galactosidase A using a baculovirus vector
JP2792813B2 (ja)	1998-09-03	新規な白血球インターフェロン
US6344547B1 (en)	2002-02-05	Human MutT2
CA2004764C (en)	1999-07-06	Ancrod proteins, their preparation and use
AU4772596A (en)	1996-08-21	Recombinant alpha-galactosidase enzyme
EP0721339A1 (en)	1996-07-17	RECOMBINANT $g(a)-GALACTOSIDASE ENZYME AND cDNA ENCODING SAID ENZYME
WO1997033903A1 (en)	1997-09-18	HUMAN MutY
US20050026249A1 (en)	2005-02-03	Enzymatically active recombinant glucocerebrosidase
Funk et al.	1990	[54] Molecular biology and cloning of archidonate 5-lipoxygenase