RECOMBINANT COLLAGEN, PREPARATION METHOD THEREFOR AND APPLICATION THEREOF
The present invention relates to recombinant collagen, a preparation method therefor and an application thereof, and in particular, to a recombinantly expressed full-length collagen α1 chain, a preparation method therefor and an application thereof, relating to the technical field of collagen expres...
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| creator | WANG, Liping LIU, Huimin LI, Jiajia QIAN, Song JIANG, Wenwen CHENG, Pengfei QIAN, Chenming |
| description | The present invention relates to recombinant collagen, a preparation method therefor and an application thereof, and in particular, to a recombinantly expressed full-length collagen α1 chain, a preparation method therefor and an application thereof, relating to the technical field of collagen expression. When a human I-type collagen α1 chain (α1(I) chain) variant (recorded as α1(I)M1) and a human II-type collagen α1 chain (α1(II) chain) variant (recorded as α1(II)M6) constructed in the present invention are recombinantly expressed in Pichia pastoris, main degradation products (main degradation bands) which are basically the same as full-length α1 chain target products (target bands) in proportion and appear during recombinant expression of natural full-length α1(I) chain and α1(II) chain are eliminated, so that the yield of the target products is increased, and compared with natural full-length α1(I) chain collagen and α1(II) chain collagen recombinantly expressed in Pichia pastoris, α1(Ⅰ)M1 and α1(Ⅱ)M6 have |
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When a human I-type collagen α1 chain (α1(I) chain) variant (recorded as α1(I)M1) and a human II-type collagen α1 chain (α1(II) chain) variant (recorded as α1(II)M6) constructed in the present invention are recombinantly expressed in Pichia pastoris, main degradation products (main degradation bands) which are basically the same as full-length α1 chain target products (target bands) in proportion and appear during recombinant expression of natural full-length α1(I) chain and α1(II) chain are eliminated, so that the yield of the target products is increased, and compared with natural full-length α1(I) chain collagen and α1(II) chain collagen recombinantly expressed in Pichia pastoris, α1(Ⅰ)M1 and α1(Ⅱ)M6 have</abstract><oa>free_for_read</oa></addata></record> |
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| subjects | BEER BIOCHEMISTRY CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS, ORSURGICAL ARTICLES CHEMISTRY COMPOSITIONS THEREOF CULTURE MEDIA DISINFECTION, STERILISATION, OR DEODORISATION OF AIR ENZYMOLOGY FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIREDCHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERSFROM A RACEMIC MIXTURE HUMAN NECESSITIES HYGIENE MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS, OR SURGICALARTICLES MEDICAL OR VETERINARY SCIENCE METALLURGY METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS INGENERAL MICROBIOLOGY MICROORGANISMS OR ENZYMES MUTATION OR GENETIC ENGINEERING ORGANIC CHEMISTRY PEPTIDES PROPAGATING, PRESERVING OR MAINTAINING MICROORGANISMS SPIRITS VINEGAR WINE |
| title | RECOMBINANT COLLAGEN, PREPARATION METHOD THEREFOR AND APPLICATION THEREOF |
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