CN106008702B - A kind of method that scale isolates and purifies recombination human source collagen - Google Patents
A kind of method that scale isolates and purifies recombination human source collagen Download PDFInfo
- Publication number
- CN106008702B CN106008702B CN201610585372.4A CN201610585372A CN106008702B CN 106008702 B CN106008702 B CN 106008702B CN 201610585372 A CN201610585372 A CN 201610585372A CN 106008702 B CN106008702 B CN 106008702B
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- CN
- China
- Prior art keywords
- human source
- recombination human
- pichia pastoris
- buffer solution
- source collagen
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- 108010035532 Collagen Proteins 0.000 title claims abstract description 37
- 102000008186 Collagen Human genes 0.000 title claims abstract description 36
- 229920001436 collagen Polymers 0.000 title claims abstract description 36
- 238000005215 recombination Methods 0.000 title claims abstract description 34
- 230000006798 recombination Effects 0.000 title claims abstract description 34
- 238000000034 method Methods 0.000 title claims abstract description 21
- 239000012535 impurity Substances 0.000 claims abstract description 21
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims abstract description 19
- 239000004202 carbamide Substances 0.000 claims abstract description 19
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 18
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 17
- 238000000108 ultra-filtration Methods 0.000 claims abstract description 13
- 238000001641 gel filtration chromatography Methods 0.000 claims abstract description 10
- 238000001471 micro-filtration Methods 0.000 claims abstract description 7
- ZMANZCXQSJIPKH-UHFFFAOYSA-N Triethylamine Chemical compound CCN(CC)CC ZMANZCXQSJIPKH-UHFFFAOYSA-N 0.000 claims description 27
- 239000007853 buffer solution Substances 0.000 claims description 18
- 239000006228 supernatant Substances 0.000 claims description 16
- 235000018102 proteins Nutrition 0.000 claims description 15
- 241000235058 Komagataella pastoris Species 0.000 claims description 13
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 claims description 12
- 229960001484 edetic acid Drugs 0.000 claims description 11
- 239000004475 Arginine Substances 0.000 claims description 10
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 claims description 10
- 239000003513 alkali Substances 0.000 claims description 10
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 10
- 239000007788 liquid Substances 0.000 claims description 10
- 150000003384 small molecules Chemical class 0.000 claims description 9
- 239000000243 solution Substances 0.000 claims description 9
- 238000000855 fermentation Methods 0.000 claims description 8
- 230000004151 fermentation Effects 0.000 claims description 8
- 229920005654 Sephadex Polymers 0.000 claims description 6
- 239000012507 Sephadex™ Substances 0.000 claims description 6
- 239000012141 concentrate Substances 0.000 claims description 6
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims description 5
- 235000018417 cysteine Nutrition 0.000 claims description 5
- 229910052757 nitrogen Inorganic materials 0.000 claims description 5
- 239000012460 protein solution Substances 0.000 claims description 5
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 claims description 2
- 239000000945 filler Substances 0.000 claims description 2
- 238000009987 spinning Methods 0.000 claims description 2
- 238000005119 centrifugation Methods 0.000 claims 2
- 239000007789 gas Substances 0.000 claims 1
- 238000011084 recovery Methods 0.000 abstract description 9
- 238000004519 manufacturing process Methods 0.000 abstract description 5
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 abstract description 4
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 abstract description 4
- 239000012528 membrane Substances 0.000 abstract description 4
- 238000011031 large-scale manufacturing process Methods 0.000 abstract description 3
- 238000000926 separation method Methods 0.000 abstract description 3
- 238000010521 absorption reaction Methods 0.000 description 4
- 238000004587 chromatography analysis Methods 0.000 description 4
- 239000000706 filtrate Substances 0.000 description 4
- 239000007791 liquid phase Substances 0.000 description 4
- 238000005374 membrane filtration Methods 0.000 description 4
- 238000009777 vacuum freeze-drying Methods 0.000 description 4
- 244000005700 microbiome Species 0.000 description 3
- 241000894006 Bacteria Species 0.000 description 2
- 241000588724 Escherichia coli Species 0.000 description 2
- 244000286779 Hansenula anomala Species 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 239000003292 glue Substances 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 1
- 235000014683 Hansenula anomala Nutrition 0.000 description 1
- 108010093096 Immobilized Enzymes Proteins 0.000 description 1
- 108010050808 Procollagen Proteins 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 239000012876 carrier material Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 239000002537 cosmetic Substances 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 230000004907 flux Effects 0.000 description 1
- 235000013373 food additive Nutrition 0.000 description 1
- 239000002778 food additive Substances 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 238000005227 gel permeation chromatography Methods 0.000 description 1
- 238000012215 gene cloning Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 238000009629 microbiological culture Methods 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000030788 protein refolding Effects 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
Classifications
-
- 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
- C07K14/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG]
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Abstract
Description
Claims (3)
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN201610585372.4A CN106008702B (en) | 2016-07-22 | 2016-07-22 | A kind of method that scale isolates and purifies recombination human source collagen |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
CN201610585372.4A CN106008702B (en) | 2016-07-22 | 2016-07-22 | A kind of method that scale isolates and purifies recombination human source collagen |
Publications (2)
Publication Number | Publication Date |
---|---|
CN106008702A CN106008702A (en) | 2016-10-12 |
CN106008702B true CN106008702B (en) | 2019-11-26 |
Family
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Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
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CN201610585372.4A Active CN106008702B (en) | 2016-07-22 | 2016-07-22 | A kind of method that scale isolates and purifies recombination human source collagen |
Country Status (1)
Country | Link |
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CN (1) | CN106008702B (en) |
Family Cites Families (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US6653098B1 (en) * | 1998-02-23 | 2003-11-25 | G. D. Searle & Co. | Method of producing mouse and human endostatin |
CN1260247C (en) * | 2003-11-05 | 2006-06-21 | 上海中科伍佰豪生物工程有限公司 | Large-scale cytorrhyctes compound purifying technology for recombining tPA derivative |
SG162834A1 (en) * | 2006-07-14 | 2010-07-29 | Genentech Inc | Refolding of recombinant proteins |
CN102443057B (en) * | 2011-10-26 | 2013-10-30 | 南京理工高新技术发展有限公司 | Recombinant humanized collagen and its preparation method |
-
2016
- 2016-07-22 CN CN201610585372.4A patent/CN106008702B/en active Active
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Publication number | Publication date |
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CN106008702A (en) | 2016-10-12 |
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Address after: 214500 Jiangsu city of Taizhou Province Jing Textile City Road No. 18 Applicant after: JIANGSU JLAND BIOTECH Co.,Ltd. Address before: 214500 Jiangsu city of Taizhou province in the eastern suburbs of Jingjiang textile Village Road on the south side of Building 2 Applicant before: JIANGSU JLAND BIOTECH Co.,Ltd. |
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CB03 | Change of inventor or designer information |
Inventor after: Yang Shulin Inventor after: Zhou Aimei Inventor after: Huang Jianmin Inventor after: Gao Lihu Inventor after: Zhao Jianfeng Inventor after: Du Erfeng Inventor after: Feng Liping Inventor after: Tao Hai Inventor after: Ji Le Inventor before: Zhou Aimei Inventor before: Huang Jianmin Inventor before: Gao Lihu Inventor before: Zhao Jianfeng Inventor before: Du Erfeng Inventor before: Feng Liping Inventor before: Tao Hai Inventor before: Ji Le |
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Address after: 214500 Jiangsu city of Taizhou province Jingjiang City Jingcheng Textile Road No. 18 Applicant after: JIANGSU JLAND BIOTECH Co.,Ltd. Address before: 214500 Jiangsu city of Taizhou Province Jing Textile City Road No. 18 Applicant before: JIANGSU JLAND BIOTECH Co.,Ltd. |
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PE01 | Entry into force of the registration of the contract for pledge of patent right | ||
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Denomination of invention: A method of large scale separation and purification of recombinant human collagen Effective date of registration: 20200922 Granted publication date: 20191126 Pledgee: Jiangsu Jingjiang Rural Commercial Bank Co.,Ltd. Pledgor: JIANGSU JLAND BIOTECH Co.,Ltd. Registration number: Y2020980006328 |
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Date of cancellation: 20221107 Granted publication date: 20191126 Pledgee: Jiangsu Jingjiang Rural Commercial Bank Co.,Ltd. Pledgor: JIANGSU JLAND BIOTECH Co.,Ltd. Registration number: Y2020980006328 |
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Effective date of registration: 20230627 Address after: 311899 No. 69, Youyi North Road, Taozhu Street, Zhuji City, Shaoxing, Zhejiang Province Patentee after: Zhejiang Zhuji Juyuan Biotechnology Co.,Ltd. Address before: 214500 No.18, Jingcheng Textile Road, Jingjiang City, Taizhou City, Jiangsu Province Patentee before: JIANGSU JLAND BIOTECH Co.,Ltd. |
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