ZA200101585B - Process for the preparation of active somatotropin from inclusion bodies. - Google Patents

Process for the preparation of active somatotropin from inclusion bodies. Download PDF

Info

Publication number: ZA200101585B
Authority: ZA; South Africa
Prior art keywords: somatotropin; inclusion bodies; alcohol; concentration; protein
Prior art date: 1998-08-27

Application number

ZA200101585A

Other languages

English (en)

Inventor

Yong Jun Lee

Hong Kyun Lee

Kyuboem Han

Original Assignee

Lg Chemical Ltd

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.)

1998-08-27

Filing date

2001-02-26

Publication date

2002-08-26

2001-02-26 Application filed by Lg Chemical Ltd filed Critical Lg Chemical Ltd

2002-08-26 Publication of ZA200101585B publication Critical patent/ZA200101585B/en

Links

238000000034 method Methods 0.000 title claims description 89
108010051696 Growth Hormone Proteins 0.000 title claims description 80
102000018997 Growth Hormone Human genes 0.000 title claims description 80
210000003000 inclusion body Anatomy 0.000 title claims description 47
238000002360 preparation method Methods 0.000 title claims description 6
KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 claims description 81
108090000623 proteins and genes Proteins 0.000 claims description 43
235000018102 proteins Nutrition 0.000 claims description 42
102000004169 proteins and genes Human genes 0.000 claims description 42
BDERNNFJNOPAEC-UHFFFAOYSA-N propan-1-ol Chemical compound CCCO BDERNNFJNOPAEC-UHFFFAOYSA-N 0.000 claims description 36
210000004027 cell Anatomy 0.000 claims description 32
239000000243 solution Substances 0.000 claims description 28
DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical group OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 claims description 17
239000003638 chemical reducing agent Substances 0.000 claims description 13
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 12
241000588724 Escherichia coli Species 0.000 claims description 11
125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 claims description 8
UFULAYFCSOUIOV-UHFFFAOYSA-N cysteamine Chemical compound NCCS UFULAYFCSOUIOV-UHFFFAOYSA-N 0.000 claims description 6
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 6
229960003151 mercaptamine Drugs 0.000 claims description 6
239000007800 oxidant agent Substances 0.000 claims description 5
239000007864 aqueous solution Substances 0.000 claims description 4
239000000203 mixture Substances 0.000 claims description 4
241000283690 Bos taurus Species 0.000 claims description 3
108010024636 Glutathione Proteins 0.000 claims description 3
XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 claims description 3
XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims description 3
235000018417 cysteine Nutrition 0.000 claims description 3
229960002433 cysteine Drugs 0.000 claims description 3
229960003180 glutathione Drugs 0.000 claims description 3
241000251468 Actinopterygii Species 0.000 claims description 2
241000972773 Aulopiformes Species 0.000 claims description 2
241000271566 Aves Species 0.000 claims description 2
241000282465 Canis Species 0.000 claims description 2
241000283707 Capra Species 0.000 claims description 2
241000282324 Felis Species 0.000 claims description 2
241000287828 Gallus gallus Species 0.000 claims description 2
241000269978 Pleuronectiformes Species 0.000 claims description 2
241001529596 Pontinus kuhlii Species 0.000 claims description 2
235000019688 fish Nutrition 0.000 claims description 2
235000019515 salmon Nutrition 0.000 claims description 2
230000003381 solubilizing effect Effects 0.000 description 32
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 21
238000010405 reoxidation reaction Methods 0.000 description 20
239000002244 precipitate Substances 0.000 description 17
239000000725 suspension Substances 0.000 description 17
239000012153 distilled water Substances 0.000 description 16
108010006025 bovine growth hormone Proteins 0.000 description 15
HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 12
230000000694 effects Effects 0.000 description 12
238000004153 renaturation Methods 0.000 description 12
230000007928 solubilization Effects 0.000 description 12
238000005063 solubilization Methods 0.000 description 12
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 10
230000015572 biosynthetic process Effects 0.000 description 9
239000003795 chemical substances by application Substances 0.000 description 8
238000000746 purification Methods 0.000 description 7
QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 6
DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 6
229960001484 edetic acid Drugs 0.000 description 6
XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 5
239000004202 carbamide Substances 0.000 description 5
239000006228 supernatant Substances 0.000 description 5
239000004094 surface-active agent Substances 0.000 description 5
238000000108 ultra-filtration Methods 0.000 description 5
-1 e.g. Substances 0.000 description 4
239000002002 slurry Substances 0.000 description 4
239000004471 Glycine Substances 0.000 description 3
239000013504 Triton X-100 Substances 0.000 description 3
229920004890 Triton X-100 Polymers 0.000 description 3
125000000539 amino acid group Chemical group 0.000 description 3
239000007788 liquid Substances 0.000 description 3
239000000178 monomer Substances 0.000 description 3
230000001590 oxidative effect Effects 0.000 description 3
239000008188 pellet Substances 0.000 description 3
238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 3
239000011541 reaction mixture Substances 0.000 description 3
MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 2
150000001413 amino acids Chemical group 0.000 description 2
238000005119 centrifugation Methods 0.000 description 2
230000003196 chaotropic effect Effects 0.000 description 2
239000012141 concentrate Substances 0.000 description 2
238000007796 conventional method Methods 0.000 description 2
238000010494 dissociation reaction Methods 0.000 description 2
230000005593 dissociations Effects 0.000 description 2
239000000706 filtrate Substances 0.000 description 2
239000012535 impurity Substances 0.000 description 2
239000000463 material Substances 0.000 description 2
244000005700 microbiome Species 0.000 description 2
230000007935 neutral effect Effects 0.000 description 2
239000002736 nonionic surfactant Substances 0.000 description 2
238000007254 oxidation reaction Methods 0.000 description 2
238000011084 recovery Methods 0.000 description 2
238000011160 research Methods 0.000 description 2
239000012465 retentate Substances 0.000 description 2
238000003756 stirring Methods 0.000 description 2
239000008215 water for injection Substances 0.000 description 2
BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 1
229910021591 Copper(I) chloride Inorganic materials 0.000 description 1
229920002271 DEAE-Sepharose Polymers 0.000 description 1
BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
150000001298 alcohols Chemical class 0.000 description 1
239000003513 alkali Substances 0.000 description 1
238000005571 anion exchange chromatography Methods 0.000 description 1
QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
239000003054 catalyst Substances 0.000 description 1
238000006243 chemical reaction Methods 0.000 description 1
230000000052 comparative effect Effects 0.000 description 1
OXBLHERUFWYNTN-UHFFFAOYSA-M copper(I) chloride Chemical compound [Cu]Cl OXBLHERUFWYNTN-UHFFFAOYSA-M 0.000 description 1
210000000805 cytoplasm Anatomy 0.000 description 1
230000001086 cytosolic effect Effects 0.000 description 1
238000007865 diluting Methods 0.000 description 1
238000010790 dilution Methods 0.000 description 1
239000012895 dilution Substances 0.000 description 1
230000002708 enhancing effect Effects 0.000 description 1
DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 1
239000000122 growth hormone Substances 0.000 description 1
150000002357 guanidines Chemical class 0.000 description 1
230000002209 hydrophobic effect Effects 0.000 description 1
238000004519 manufacturing process Methods 0.000 description 1
239000012528 membrane Substances 0.000 description 1
229910052751 metal Inorganic materials 0.000 description 1
239000002184 metal Substances 0.000 description 1
230000000813 microbial effect Effects 0.000 description 1
238000012986 modification Methods 0.000 description 1
230000004048 modification Effects 0.000 description 1
125000004123 n-propyl group Chemical group [H]C([H])([H])C([H])([H])C([H])([H])* 0.000 description 1
230000003647 oxidation Effects 0.000 description 1
239000001301 oxygen Substances 0.000 description 1
229910052760 oxygen Inorganic materials 0.000 description 1
230000001737 promoting effect Effects 0.000 description 1
239000013636 protein dimer Substances 0.000 description 1
238000001742 protein purification Methods 0.000 description 1
238000011002 quantification Methods 0.000 description 1
239000011780 sodium chloride Substances 0.000 description 1
239000007787 solid Substances 0.000 description 1
230000006641 stabilisation Effects 0.000 description 1
238000011105 stabilization Methods 0.000 description 1
239000000126 substance Substances 0.000 description 1
230000002277 temperature effect Effects 0.000 description 1
239000013638 trimer Substances 0.000 description 1
GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
210000005253 yeast cell Anatomy 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
- C07K1/113—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure
- C07K1/1133—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure by redox-reactions involving cystein/cystin side chains
- 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
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/61—Growth hormone [GH], i.e. somatotropin
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/82—Proteins from microorganisms
- Y10S530/823—Lower fungi, e.g. mold
- Y10S530/824—Yeasts
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/82—Proteins from microorganisms
- Y10S530/825—Bacteria

Landscapes

Chemical & Material Sciences (AREA)
Health & Medical Sciences (AREA)
Organic Chemistry (AREA)
Life Sciences & Earth Sciences (AREA)
Genetics & Genomics (AREA)
General Health & Medical Sciences (AREA)
Biochemistry (AREA)
Molecular Biology (AREA)
Biophysics (AREA)
Endocrinology (AREA)
Zoology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Medicinal Chemistry (AREA)
Chemical Kinetics & Catalysis (AREA)
Engineering & Computer Science (AREA)
Wood Science & Technology (AREA)
Gastroenterology & Hepatology (AREA)
General Chemical & Material Sciences (AREA)
Biomedical Technology (AREA)
Toxicology (AREA)
Analytical Chemistry (AREA)
Bioinformatics & Cheminformatics (AREA)
Biotechnology (AREA)
Cell Biology (AREA)
General Engineering & Computer Science (AREA)
Microbiology (AREA)
Peptides Or Proteins (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)

ZA200101585A 1998-08-27 2001-02-26 Process for the preparation of active somatotropin from inclusion bodies. ZA200101585B (en)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
KR19980034910		1998-08-27

Publications (1)

Publication Number	Publication Date
ZA200101585B true ZA200101585B (en)	2002-08-26

Family

ID=19548527

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
ZA200101585A ZA200101585B (en)	1998-08-27	2001-02-26	Process for the preparation of active somatotropin from inclusion bodies.

Country Status (6)

Country	Link
US (1)	US6987173B2 (pt)
KR (1)	KR100327040B1 (pt)
AU (1)	AU739394B2 (pt)
BR (1)	BRPI9913018B8 (pt)
WO (1)	WO2000012537A1 (pt)
ZA (1)	ZA200101585B (pt)

Families Citing this family (6)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
PL213561B1 (pl) *	2004-01-09	2013-03-29	Inst Biotechnologii I Antybiotykow	Sposób otrzymywania plazmidu, plazmid oraz zastosowania
ITPR20040015A1 (it) *	2004-02-24	2004-05-24	Niro Soavi Spa	Procedimento e apparato per la rottura cellulare in una sospensione fluida in continuo.
EP1720897B1 (en)	2004-02-27	2010-03-31	Dow Global Technologies Inc.	Method for the extraction of intracellular proteins from a fermentation broth
PT3597659T (pt)	2007-07-09	2023-04-04	Genentech Inc	Prevenção da redução de ligações de dissulfureto durante a produção recombinante de polipéptidos
BR102013026129A2 (pt) *	2013-10-10	2016-05-24	Ouro Fino Participações E Empreendimentos S A	processo para a produção de somatotropina bovina recombinate ativa e produto obtido
CN112062810A (zh) *	2020-09-29	2020-12-11	北京中源合聚生物科技有限公司	一种包涵体复性集约装置

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
ES2062253T3 (es) *	1989-12-05	1994-12-16	American Cyanamid Co	Metodo para solubilizacion y naturalizacion de somatotropinas utilizando una baja concentracion de urea.
US5109117A (en) *	1990-06-26	1992-04-28	Monsanto Company	Method of somatotropin naturation using urea and a soluble organic alcohol
WO1994001453A1 (en) *	1992-07-02	1994-01-20	Pitman-Moore, Inc.	A process for recovering a recombinant protein, in biologically active form, from a solution containing inactive protein

1999
- 1999-08-26 AU AU55303/99A patent/AU739394B2/en not_active Ceased
- 1999-08-26 BR BRPI9913018-1 patent/BRPI9913018B8/pt unknown
- 1999-08-26 WO PCT/KR1999/000485 patent/WO2000012537A1/en active IP Right Grant
- 1999-08-27 KR KR1019990035982A patent/KR100327040B1/ko not_active IP Right Cessation
2001
- 2001-01-12 US US09/811,789 patent/US6987173B2/en not_active Expired - Fee Related
- 2001-02-26 ZA ZA200101585A patent/ZA200101585B/en unknown

Also Published As

Publication number	Publication date
KR20000017601A (ko)	2000-03-25
BRPI9913018B8 (pt)	2021-07-06
KR100327040B1 (ko)	2002-03-06
AU5530399A (en)	2000-03-21
WO2000012537A1 (en)	2000-03-09
BRPI9913018A (pt)	2001-05-08
AU739394B2 (en)	2001-10-11
US6987173B2 (en)	2006-01-17
BRPI9913018B1 (pt)	2011-07-26
US20030229210A1 (en)	2003-12-11

Publication	Publication Date	Title
EP0714406B1 (en)	2004-04-21	Refolding of polypeptides like recombinant insulin-like growth factor igf-i
EP0212960B1 (en)	1993-07-07	Purification and activation of proteins from insoluble inclusion bodies
EP0215625B1 (en)	1994-11-09	Protein recovery
Samuelsson et al.	1991	Facilitated in vitro refolding of human recombinant insulin-like growth factor I using a solubilizing fusion partner
US5064943A (en)	1991-11-12	Method for solubilization and naturation of somatotropin
US6987173B2 (en)	2006-01-17	Process for the preparation of active somatotropin from inclusion bodies
US9296806B2 (en)	2016-03-29	Processes for refolding of insulin
US4705848A (en)	1987-11-10	Isolation of bioactive, monomeric growth hormone
JP3930051B2 (ja)	2007-06-13	正しく折畳まれた生物学的に活性の組換えタンパク質の製造方法
JPH06104070B2 (ja)	1994-12-21	形質転換した微生物からのソマトトロピンの精製
US6034224A (en)	2000-03-07	Method for solubilization and naturation of somatotropins
MXPA01001168A (en)	2001-11-21	Process for the preparation of active somatotropin from inclusion bodies
RU2123010C1 (ru)	1998-12-10	Способ получения рекомбинантного интерферона-альфа-2 из нерастворимых тел включения