RU2014114954A - Recombinant DNA pA4, recombinant DNA pQE 30-pA4, produces the polypeptide A4, STRAIN Esherichia coli M 15-A4, transformed with recombinant plasmid DNA of pQE 30-pA4 and expression of recombinant polypeptides A4, recombinant polypeptides A4, has the ability to selectively bind HSA affinity sorbent (OPTIONS) AND METHODS FOR REMOVING HSA AND IgG FROM BLOOD SERUM (OPTIONS) - Google Patents
Recombinant DNA pA4, recombinant DNA pQE 30-pA4, produces the polypeptide A4, STRAIN Esherichia coli M 15-A4, transformed with recombinant plasmid DNA of pQE 30-pA4 and expression of recombinant polypeptides A4, recombinant polypeptides A4, has the ability to selectively bind HSA affinity sorbent (OPTIONS) AND METHODS FOR REMOVING HSA AND IgG FROM BLOOD SERUM (OPTIONS) Download PDFInfo
- Publication number
- RU2014114954A RU2014114954A RU2014114954/10A RU2014114954A RU2014114954A RU 2014114954 A RU2014114954 A RU 2014114954A RU 2014114954/10 A RU2014114954/10 A RU 2014114954/10A RU 2014114954 A RU2014114954 A RU 2014114954A RU 2014114954 A RU2014114954 A RU 2014114954A
- Authority
- RU
- Russia
- Prior art keywords
- recombinant
- dna
- pqe
- hsa
- polypeptide
- Prior art date
Links
Landscapes
- Peptides Or Proteins (AREA)
- Solid-Sorbent Or Filter-Aiding Compositions (AREA)
- External Artificial Organs (AREA)
Abstract
1. Рекомбинантная ДНК рА4, нуклеотидная последовательность которой составляет 612 п.н.2. Рекомбинантная ДНК pQE 30-pA4, представляющая собой плазмиду pQE 30, несущую рекомбинантную ДНК рА4, и обеспечивающая получение полипептида А4.3. Штамм Esherichia coli M 15-A4, трансформированный рекомбинантной плазмидной ДНК pQE 30-pA4 и экспрессирующий рекомбинантный полипептид А4.4. Рекомбинантный полипептид А4, обладающий способностью селективно связывать ЧСА.5. Аффинный сорбент, в котором к матрице, представляющей собой активированную цианбромом сефарозу 4В присоединен ЧСА-связывающий полипептид.6. Аффинный комбинированный сорбент, состоящий одновременно из двух сорбентов: сефарозы 4В-IgG-связывающего полипептида и сорбента по п.5.7. Способ последовательного удаления ЧСА и IgG из сыворотки крови методом аффинной хроматографии, отличающийся тем, что в качестве аффинных носителей в последовательно соединенных колонках используются сефароза 4В-IgG-связывающий полипептид и сорбент по п.5.8. Способ одновременного удаления ЧСА и IgG из сыворотки крови, отличающийся тем, что в качестве сорбента используют аффинный комбинированный сорбент по п.6.1. Recombinant pA4 DNA, the nucleotide sequence of which is 612 bp. 2. Recombinant DNA pQE 30-pA4, which is a plasmid pQE 30, carrying recombinant pA4 DNA, and providing the production of A4.3 polypeptide. The strain Esherichia coli M 15-A4, transformed with recombinant plasmid DNA pQE 30-pA4 and expressing the recombinant polypeptide A4.4. Recombinant A4 polypeptide with the ability to selectively bind HSA. 5. An affinity sorbent in which an HSA-binding polypeptide is attached to a matrix of cyanbrom-activated 4B sepharose 4B. An affinity combined sorbent consisting simultaneously of two sorbents: Sepharose 4B-IgG-binding polypeptide and the sorbent according to clause 5.7. The method of sequential removal of HSA and IgG from blood serum by affinity chromatography, characterized in that sepharose 4B-IgG-binding polypeptide and sorbent according to claim 5.8 are used as affinity carriers in series-connected columns. A method for the simultaneous removal of HSA and IgG from blood serum, characterized in that the affinity combined sorbent according to claim 6 is used as the sorbent.
Claims (8)
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
RU2014114954/10A RU2572343C2 (en) | 2014-04-15 | 2014-04-15 | RECOMBINANT DNA pA4, RECOMBINANT DNA pQE 30-pA4, PROVIDING OBTAINING POLYPEPTIDE A4, Esherichia coli STRAIN M 15-A4, TRANSFORMED WITH RECOMBINANT PLASMID DNA pQE 30-pA4, AND EXPRESSING RECOMBINANT POLYPEPTIDE A4, RECOMBINANT POLYPEPTIDE A4, POSSESSING ABILITY TO SELECTIVELY BIND HSA, AFFINE SORBENTS (VERSIONS) AND METHODS FOR HSA AND IgG REMOVAL FROM BLOOD SERUM (VERSIONS) |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
RU2014114954/10A RU2572343C2 (en) | 2014-04-15 | 2014-04-15 | RECOMBINANT DNA pA4, RECOMBINANT DNA pQE 30-pA4, PROVIDING OBTAINING POLYPEPTIDE A4, Esherichia coli STRAIN M 15-A4, TRANSFORMED WITH RECOMBINANT PLASMID DNA pQE 30-pA4, AND EXPRESSING RECOMBINANT POLYPEPTIDE A4, RECOMBINANT POLYPEPTIDE A4, POSSESSING ABILITY TO SELECTIVELY BIND HSA, AFFINE SORBENTS (VERSIONS) AND METHODS FOR HSA AND IgG REMOVAL FROM BLOOD SERUM (VERSIONS) |
Publications (2)
Publication Number | Publication Date |
---|---|
RU2014114954A true RU2014114954A (en) | 2015-10-20 |
RU2572343C2 RU2572343C2 (en) | 2016-01-10 |
Family
ID=54326962
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
RU2014114954/10A RU2572343C2 (en) | 2014-04-15 | 2014-04-15 | RECOMBINANT DNA pA4, RECOMBINANT DNA pQE 30-pA4, PROVIDING OBTAINING POLYPEPTIDE A4, Esherichia coli STRAIN M 15-A4, TRANSFORMED WITH RECOMBINANT PLASMID DNA pQE 30-pA4, AND EXPRESSING RECOMBINANT POLYPEPTIDE A4, RECOMBINANT POLYPEPTIDE A4, POSSESSING ABILITY TO SELECTIVELY BIND HSA, AFFINE SORBENTS (VERSIONS) AND METHODS FOR HSA AND IgG REMOVAL FROM BLOOD SERUM (VERSIONS) |
Country Status (1)
Country | Link |
---|---|
RU (1) | RU2572343C2 (en) |
Families Citing this family (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
RU2715672C2 (en) * | 2017-12-26 | 2020-03-02 | Федеральное государственное бюджетное научное учреждение "Институт экспериментальной медицины" (ФГБНУ "ИЭМ") | RECOMBINANT DNA OF pG4223 AND PLASMID DNA PQE 30-pG4223, STRAIN OF ESCHERICHIA COLI M 15-G4223 WHICH ENABLE TO OBTAIN G4223 POLYPEPTIDE SELECTIVELY BINDING IgG, AND USE THEREOF IN AFFINE CHROMATOGRAPHY TO ISOLATE IgG |
RU2758604C2 (en) * | 2019-12-10 | 2021-11-01 | Федеральное государственное бюджетное научное учреждение "Институт экспериментальной медицины" (ФГБНУ "ИЭМ") | Recombinant gm protein capable of binding α2-macroglobulin and application thereof as a ligand in affinity chromatography for extracting α2-macroglobulin from human blood serum |
Family Cites Families (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
SU734215A1 (en) * | 1977-10-24 | 1980-05-15 | Институт Биохимии Им.А.В.Палладина Ан Укринской Сср | Method of preparing sorbents for affinic chromatography of serine proteases |
RU2056859C1 (en) * | 1993-12-14 | 1996-03-27 | Татьяна Витальевна Гупалова | Recombinant igg-binding g-protein of streptococcus |
-
2014
- 2014-04-15 RU RU2014114954/10A patent/RU2572343C2/en not_active IP Right Cessation
Also Published As
Publication number | Publication date |
---|---|
RU2572343C2 (en) | 2016-01-10 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
WO2015195453A3 (en) | Methods for increasing the capacity of flow-through processes | |
HRP20191865T1 (en) | Novel heterodimeric proteins | |
EA201891420A1 (en) | ANTIBODIES TO MYOSTATIN, POLYPEPTIDES, CONTAINING OPTIONS OF FC-REGIONS, AND METHODS OF THEIR APPLICATION | |
AR092050A1 (en) | FUSION PROTEINS OF ANTIBODIES AND INTERLEUQUINE 10 AND USES OF THE SAME | |
WO2018085599A3 (en) | Methods of nucleic acid sample preparation for immune repertoire sequencing | |
MY194669A (en) | Binding Proteins and Methods of use Thereof | |
WO2017201432A3 (en) | Tethered interleukin-2 to its receptor il-2rbeta, a platform to enhance natural killer and regulatory t cell activity | |
MX2017014397A (en) | Anti-fcrn antibodies. | |
PH12015502125A1 (en) | Il-22 polypeptides and il-22 fc fusion proteins and methods of use | |
WO2014018858A3 (en) | Multimeric fusion protein vaccine and immunotherapeutic | |
AR099288A1 (en) | INTERLEUCINE FUSION PROTEINS-10 | |
EA201491494A1 (en) | NACELIVANIE NA GLIKANY HONDROITINSULFATY | |
MX348071B (en) | Fc variants. | |
SG10201808738WA (en) | Fusokines involving cytokines with strongly reduced receptor binding affinities | |
AR104358A1 (en) | METHOD FOR PROTEIN PURIFICATION | |
WO2015140638A8 (en) | Glycosylated vegf decoy receptor fusion protein | |
WO2016073794A8 (en) | Methods of producing two chain proteins in bacteria | |
MX2021001418A (en) | Production of heteromultimeric proteins using mammalian cells. | |
EA201690205A1 (en) | SITE-SPECIFIC CHEMICAL-ENMENTATIVE MODIFICATIONS OF PROTEINS | |
WO2017019565A3 (en) | Fusion proteins of human protein fragments to create orderly multimerized immunoglobulin fc compositions with enhanced complement binding | |
MX2015000754A (en) | Human btnl3 proteins, nucleic acids, and antibodies and uses thereof. | |
SG10201807572PA (en) | Robust antibody purification | |
MA49769A (en) | PROTEINS BINDING TO NKG2D, CD16 AND FLT3 | |
WO2016044436A3 (en) | Anti-vasa antibodies, and methods of production and use thereof | |
RU2014114954A (en) | Recombinant DNA pA4, recombinant DNA pQE 30-pA4, produces the polypeptide A4, STRAIN Esherichia coli M 15-A4, transformed with recombinant plasmid DNA of pQE 30-pA4 and expression of recombinant polypeptides A4, recombinant polypeptides A4, has the ability to selectively bind HSA affinity sorbent (OPTIONS) AND METHODS FOR REMOVING HSA AND IgG FROM BLOOD SERUM (OPTIONS) |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
MM4A | The patent is invalid due to non-payment of fees |
Effective date: 20170416 |