Strategies for improving expression of recombinant human chorionic gonadotropin in Chinese Hamster Ovary (CHO) cells
Optimizations of the gene expression cassette combined with the selection of an appropriate signal peptide are important factors that must be considered to enhance heterologous protein expression in Chinese Hamster Ovary (CHO) cells. In this study, we investigated the effectiveness of different sign...
Uloženo v:
| Vydáno v: | Protein expression and purification Ročník 225; s. 106596 |
|---|---|
| Hlavní autoři: | , , , , |
| Médium: | Journal Article |
| Jazyk: | angličtina |
| Vydáno: |
United States
Elsevier Inc
01.01.2025
|
| Témata: | |
| ISSN: | 1046-5928, 1096-0279, 1096-0279 |
| On-line přístup: | Získat plný text |
| Tagy: |
Přidat tag
Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!
|
| Abstract | Optimizations of the gene expression cassette combined with the selection of an appropriate signal peptide are important factors that must be considered to enhance heterologous protein expression in Chinese Hamster Ovary (CHO) cells. In this study, we investigated the effectiveness of different signal peptides on the production of recombinant human chorionic gonadotropin (r-hCG) in CHO-K1 cells. Four optimized expression constructs containing four promising signal peptides were stably transfected into CHO-K1 cells. The generated CHO-K1 stable pool was then evaluated for r-hCG protein production. Interestingly, human serum albumin and human interleukin-2 signal peptides exhibited relatively greater extracellular secretion of the r-hCG with an average yield of (16.59 ± 0.02 μg/ml) and (14.80 ± 0.13 μg/ml) respectively compared to the native and murine IgGκ light chain signal peptides. The stably transfected CHO pool was further used as the cell substrate to develop an optimized upstream process followed by a downstream phase of the r-hCG. Finally, the biological activity of the purified r-hCG was assessed using in vitro bioassays. The combined data highlight that the choice of signal peptide can be imperative to ensure an optimal secretion of a recombinant protein in CHO cells. In addition, the stable pool technology was a viable approach for the production of biologically active r-hCG at a research scale with acceptable bioprocess performances and consistent product quality.
•We developed a highly efficient approach for producing recombinant human chorionic gonadotropin (r-hCG) in CHO cells.•We highlighted the importance of selecting an appropriate signal peptide for enhancing r-hCG expression in CHO cells.•Stable pool technology yields high-quality, biologically active r-hCG at the research scale, ensuring efficiency and consistent performance. |
|---|---|
| AbstractList | Optimizations of the gene expression cassette combined with the selection of an appropriate signal peptide are important factors that must be considered to enhance heterologous protein expression in Chinese Hamster Ovary (CHO) cells. In this study, we investigated the effectiveness of different signal peptides on the production of recombinant human chorionic gonadotropin (r-hCG) in CHO-K1 cells. Four optimized expression constructs containing four promising signal peptides were stably transfected into CHO-K1 cells. The generated CHO-K1 stable pool was then evaluated for r-hCG protein production. Interestingly, human serum albumin and human interleukin-2 signal peptides exhibited relatively greater extracellular secretion of the r-hCG with an average yield of (16.59 ± 0.02 μg/ml) and (14.80 ± 0.13 μg/ml) respectively compared to the native and murine IgGκ light chain signal peptides. The stably transfected CHO pool was further used as the cell substrate to develop an optimized upstream process followed by a downstream phase of the r-hCG. Finally, the biological activity of the purified r-hCG was assessed using in vitro bioassays. The combined data highlight that the choice of signal peptide can be imperative to ensure an optimal secretion of a recombinant protein in CHO cells. In addition, the stable pool technology was a viable approach for the production of biologically active r-hCG at a research scale with acceptable bioprocess performances and consistent product quality. Optimizations of the gene expression cassette combined with the selection of an appropriate signal peptide are important factors that must be considered to enhance heterologous protein expression in Chinese Hamster Ovary (CHO) cells. In this study, we investigated the effectiveness of different signal peptides on the production of recombinant human chorionic gonadotropin (r-hCG) in CHO-K1 cells. Four optimized expression constructs containing four promising signal peptides were stably transfected into CHO-K1 cells. The generated CHO-K1 stable pool was then evaluated for r-hCG protein production. Interestingly, human serum albumin and human interleukin-2 signal peptides exhibited relatively greater extracellular secretion of the r-hCG with an average yield of (16.59 ± 0.02 μg/ml) and (14.80 ± 0.13 μg/ml) respectively compared to the native and murine IgGκ light chain signal peptides. The stably transfected CHO pool was further used as the cell substrate to develop an optimized upstream process followed by a downstream phase of the r-hCG. Finally, the biological activity of the purified r-hCG was assessed using in vitro bioassays. The combined data highlight that the choice of signal peptide can be imperative to ensure an optimal secretion of a recombinant protein in CHO cells. In addition, the stable pool technology was a viable approach for the production of biologically active r-hCG at a research scale with acceptable bioprocess performances and consistent product quality.Optimizations of the gene expression cassette combined with the selection of an appropriate signal peptide are important factors that must be considered to enhance heterologous protein expression in Chinese Hamster Ovary (CHO) cells. In this study, we investigated the effectiveness of different signal peptides on the production of recombinant human chorionic gonadotropin (r-hCG) in CHO-K1 cells. Four optimized expression constructs containing four promising signal peptides were stably transfected into CHO-K1 cells. The generated CHO-K1 stable pool was then evaluated for r-hCG protein production. Interestingly, human serum albumin and human interleukin-2 signal peptides exhibited relatively greater extracellular secretion of the r-hCG with an average yield of (16.59 ± 0.02 μg/ml) and (14.80 ± 0.13 μg/ml) respectively compared to the native and murine IgGκ light chain signal peptides. The stably transfected CHO pool was further used as the cell substrate to develop an optimized upstream process followed by a downstream phase of the r-hCG. Finally, the biological activity of the purified r-hCG was assessed using in vitro bioassays. The combined data highlight that the choice of signal peptide can be imperative to ensure an optimal secretion of a recombinant protein in CHO cells. In addition, the stable pool technology was a viable approach for the production of biologically active r-hCG at a research scale with acceptable bioprocess performances and consistent product quality. Optimizations of the gene expression cassette combined with the selection of an appropriate signal peptide are important factors that must be considered to enhance heterologous protein expression in Chinese Hamster Ovary (CHO) cells. In this study, we investigated the effectiveness of different signal peptides on the production of recombinant human chorionic gonadotropin (r-hCG) in CHO-K1 cells. Four optimized expression constructs containing four promising signal peptides were stably transfected into CHO-K1 cells. The generated CHO-K1 stable pool was then evaluated for r-hCG protein production. Interestingly, human serum albumin and human interleukin-2 signal peptides exhibited relatively greater extracellular secretion of the r-hCG with an average yield of (16.59 ± 0.02 μg/ml) and (14.80 ± 0.13 μg/ml) respectively compared to the native and murine IgGκ light chain signal peptides. The stably transfected CHO pool was further used as the cell substrate to develop an optimized upstream process followed by a downstream phase of the r-hCG. Finally, the biological activity of the purified r-hCG was assessed using in vitro bioassays. The combined data highlight that the choice of signal peptide can be imperative to ensure an optimal secretion of a recombinant protein in CHO cells. In addition, the stable pool technology was a viable approach for the production of biologically active r-hCG at a research scale with acceptable bioprocess performances and consistent product quality. •We developed a highly efficient approach for producing recombinant human chorionic gonadotropin (r-hCG) in CHO cells.•We highlighted the importance of selecting an appropriate signal peptide for enhancing r-hCG expression in CHO cells.•Stable pool technology yields high-quality, biologically active r-hCG at the research scale, ensuring efficiency and consistent performance. |
| ArticleNumber | 106596 |
| Author | Rourou, Samia Essafi-Benkhadir, Khadija Bouzazi, Dorsaf Boukari, Iheb Kallel, Héla |
| Author_xml | – sequence: 1 givenname: Iheb orcidid: 0009-0007-3831-0679 surname: Boukari fullname: Boukari, Iheb email: iheb.boukari@fsb.ucar.tn organization: Laboratory of Molecular Microbiology, Vaccinology and Biotechnology Development, LR16IPT01, Biotechnology Development Group, Institut Pasteur de Tunis, University of Tunis El Manar, 1002, Tunis, Tunisia – sequence: 2 givenname: Samia surname: Rourou fullname: Rourou, Samia organization: Laboratory of Molecular Microbiology, Vaccinology and Biotechnology Development, LR16IPT01, Biotechnology Development Group, Institut Pasteur de Tunis, University of Tunis El Manar, 1002, Tunis, Tunisia – sequence: 3 givenname: Dorsaf surname: Bouzazi fullname: Bouzazi, Dorsaf organization: Plateforme de Physiologie et Physiopathologie Cardiovasculaires, Institut Pasteur de Tunis, University of Tunis El Manar, 1002, Tunis, Tunisia – sequence: 4 givenname: Khadija surname: Essafi-Benkhadir fullname: Essafi-Benkhadir, Khadija organization: Laboratory of Molecular Epidemiology and Experimental Pathology, LR16IPT04, Institut Pasteur de Tunis, University of Tunis El Manar, 1002, Tunis, Tunisia – sequence: 5 givenname: Héla surname: Kallel fullname: Kallel, Héla organization: Laboratory of Molecular Microbiology, Vaccinology and Biotechnology Development, LR16IPT01, Biotechnology Development Group, Institut Pasteur de Tunis, University of Tunis El Manar, 1002, Tunis, Tunisia |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/39218246$$D View this record in MEDLINE/PubMed |
| BookMark | eNp9kU9rGzEQxUVJyb_mA_RSdEwP646kXe2Knopp60LAh6RnodXO2jJeaSvJJv32lXFy6SEgkAa9N8y83w258MEjIR8ZLBgw-WW3mHFecOB1qWWj5DtyzUDJCnirLk7vWlaN4t0VuUlpB8CYhOaSXAnFWcdreU3yY44m48ZhomOI1E1zDEfnNxSf54gpueBpGGlEG6beeeMz3R4m46ndhlg-naWb4M0Qcgyz87Sc5dZ5TEhXZkoZI10fTfxL75er9Wdqcb9PH8j70ewT3r3ct-T3j-9Py1X1sP75a_ntobKiEbkSKIEhY70RI2sMoG1Rqto20HLZqa4XHKEGCUPf9tAo6G09jGaUBru-rgdxS-7PfctOfw6Ysp5cOk1gPIZD0gKU6hrJRV2kn16kh37CQc_RTWVq_ZpUEbRngY0hpYijti6bXBIoAbq9ZqBPTPROFyb6xESfmRQn-8_52vwtz9ezB0s8R4dRJ-vQWxxcIZH1ENwb7n-416UO |
| CitedBy_id | crossref_primary_10_3389_fvets_2025_1530870 crossref_primary_10_1038_s41598_024_76995_6 |
| Cites_doi | 10.1016/j.procbio.2022.04.023 10.1016/j.ijgo.2013.09.005 10.1002/biot.201700268 10.1093/humupd/dmn036 10.1016/j.pep.2017.04.013 10.1016/j.jbiotec.2014.12.005 10.4103/jhrs.JHRS_101_18 10.1002/biot.201400665 10.1016/S0021-9258(18)71649-9 10.3390/ijms18102037 10.1016/j.pep.2015.10.012 10.3390/v13112160 10.1677/jme.0.0220273 10.1186/1477-7827-10-24 10.1007/s00253-011-3758-5 10.1016/j.biotechadv.2011.08.022 10.1016/j.pep.2015.02.002 10.1080/21655979.2016.1176656 10.1016/j.mce.2018.09.006 10.1016/S0021-9258(19)41303-3 10.6061/clinics/2013(Sup01)09 10.1002/btpr.469 10.1002/jgm.677 10.1039/C3AN02245E 10.1016/j.copbio.2014.06.010 10.2165/00024677-200403060-00005 10.1016/j.pep.2017.01.003 10.1007/s00253-022-12342-x 10.1002/bit.24776 10.1210/jc.2002-020642 10.1016/S0021-9258(19)77701-1 10.1016/j.jbiotec.2006.11.026 10.1016/S0167-7306(03)38026-3 10.1038/s41580-020-00294-x 10.1002/btpr.2307 10.1016/j.fertnstert.2005.02.033 10.1007/978-1-4939-6972-2_2 |
| ContentType | Journal Article |
| Copyright | 2024 Elsevier Inc. Copyright © 2024 Elsevier Inc. All rights reserved. |
| Copyright_xml | – notice: 2024 Elsevier Inc. – notice: Copyright © 2024 Elsevier Inc. All rights reserved. |
| DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 7X8 |
| DOI | 10.1016/j.pep.2024.106596 |
| DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed MEDLINE - Academic |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) MEDLINE - Academic |
| DatabaseTitleList | MEDLINE MEDLINE - Academic |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: 7X8 name: MEDLINE - Academic url: https://search.proquest.com/medline sourceTypes: Aggregation Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Anatomy & Physiology Chemistry |
| EISSN | 1096-0279 |
| ExternalDocumentID | 39218246 10_1016_j_pep_2024_106596 S1046592824001682 |
| Genre | Journal Article |
| GroupedDBID | --- --K --M .~1 0R~ 123 1B1 1RT 1~. 1~5 29P 4.4 457 4G. 53G 5VS 7-5 71M 8P~ 9JM AAAJQ AABNK AACTN AAEDT AAEDW AAIKJ AAKOC AALRI AAOAW AAQFI AAQXK AARKO AAXKI AAXUO ABFNM ABFRF ABGSF ABJNI ABMAC ABOCM ABUDA ABXDB ACDAQ ACGFO ACGFS ACRLP ADBBV ADEZE ADFGL ADMUD ADUVX AEBSH AEFWE AEHWI AEKER AENEX AFKWA AFTJW AFXIZ AGEKW AGHFR AGRDE AGUBO AGYEJ AHHHB AIEXJ AIKHN AITUG AJOXV AKRWK ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ ASPBG AVWKF AXJTR AZFZN BKOJK BLXMC CAG CJTIS COF CS3 DM4 DU5 EBS EFBJH EJD EO8 EO9 EP2 EP3 F5P FDB FEDTE FGOYB FIRID FNPLU FYGXN G-2 G-Q GBLVA HLW HVGLF HZ~ IH2 IHE J1W KOM LG5 LUGTX LX2 M41 MO0 N9A O-L O9- OAUVE OZT P-8 P-9 P2P PC. Q38 R2- RIG ROL RPZ SBG SCC SDF SDG SDP SES SEW SPCBC SSI SSU SSZ T5K WUQ XPP Y6R ZGI ZMT ZU3 ~02 ~G- 9DU AATTM AAYWO AAYXX ABWVN ACLOT ACRPL ACVFH ADCNI ADNMO AEIPS AEUPX AFJKZ AFPUW AGQPQ AIGII AIIUN AKBMS AKYEP ANKPU APXCP CITATION EFKBS EFLBG ~HD AGCQF AGRNS BNPGV CGR CUY CVF ECM EIF NPM SSH 7X8 |
| ID | FETCH-LOGICAL-c353t-3e601e11ba3f15a0ec7e694c50726898b32e04060db7b0590bc4dfaf6ae8b44d3 |
| ISICitedReferencesCount | 3 |
| ISICitedReferencesURI | http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=001306816900001&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| ISSN | 1046-5928 1096-0279 |
| IngestDate | Sun Sep 28 08:31:10 EDT 2025 Mon Jul 21 06:03:31 EDT 2025 Sat Nov 29 06:31:29 EST 2025 Tue Nov 18 22:08:46 EST 2025 Sat Sep 14 18:13:24 EDT 2024 |
| IsPeerReviewed | true |
| IsScholarly | true |
| Keywords | Signal peptide Stable pool. bioprocess optimization CHO cells Human chorionic gonadotropin |
| Language | English |
| License | Copyright © 2024 Elsevier Inc. All rights reserved. |
| LinkModel | OpenURL |
| MergedId | FETCHMERGED-LOGICAL-c353t-3e601e11ba3f15a0ec7e694c50726898b32e04060db7b0590bc4dfaf6ae8b44d3 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| ORCID | 0009-0007-3831-0679 |
| PMID | 39218246 |
| PQID | 3099856234 |
| PQPubID | 23479 |
| ParticipantIDs | proquest_miscellaneous_3099856234 pubmed_primary_39218246 crossref_citationtrail_10_1016_j_pep_2024_106596 crossref_primary_10_1016_j_pep_2024_106596 elsevier_sciencedirect_doi_10_1016_j_pep_2024_106596 |
| PublicationCentury | 2000 |
| PublicationDate | January 2025 2025-01-00 2025-Jan 20250101 |
| PublicationDateYYYYMMDD | 2025-01-01 |
| PublicationDate_xml | – month: 01 year: 2025 text: January 2025 |
| PublicationDecade | 2020 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States |
| PublicationTitle | Protein expression and purification |
| PublicationTitleAlternate | Protein Expr Purif |
| PublicationYear | 2025 |
| Publisher | Elsevier Inc |
| Publisher_xml | – name: Elsevier Inc |
| References | Schjoldager, Narimatsu, Joshi, Clausen (bib10) 2020; 21 Chen, Zhao, Zhang, Yuan, Ge, Tang, Xu, Cao, Guo (bib34) 2016; 118 Urli, Panian, Facchine, Steadman, Brankston, Borcky, Xu, Liu (bib4) 2015 Peng, Yu, Li, Cai, Chen, He, Yang, Jin, Li (bib35) 2016; 7 Cumming (bib43) 2003; 38 Zhu (bib6) 2012; 30 Ramezani, Maymand, Yazdanpanah-Samani, Hosseini, Toghraie, Ghaderi (bib29) 2017; 135 Zhang, Leng, Mixson (bib33) 2005; 7 Cho, Oh, Kim, Lim, Park, Hwang, Baek, Kim, Choi, Lee (bib22) 2019 Ye, Alvin, Latif, Hsu, Parikh, Whitmer, Tellers, de la Cruz Edmonds, Ly, Salmon (bib26) 2010; 26 Attallah, Etcheverrigaray, Kratje, Oggero (bib30) 2017; 132 Stramaglia, Fike, Naumovich, Zhao (bib19) 2008 Lin, Neo, Ho, Yeo, Wang, Zhang, Bi, Chao, Yang (bib24) 2017; 12 Inouye, Sahara-Miura, Sato, Suzuki (bib25) 2015; 109 Fournier (bib9) 2016 Kantardjieff, Zhou (bib2) 2014 Majumdar, Sachan, Nandanwar, Mayekar, Soni, Banker, Vaidya, Arora, Godbole, Daftary (bib16) 2019; 12 Gupta, Dighe (bib37) 1999; 22 Zhang (bib7) 2010 Fraietta, Zylberstejn, Esteves (bib13) 2013; 68 Alves, Dobrowsky (bib18) 2017 Kober, Zehe, Bode (bib20) 2013; 110 Kim, Kim, Lee (bib3) 2012; 93 Wang, Yin, Chung, Betenbaugh (bib48) 2017 Spellman, Basa, Leonard, Chakel, O'Connor, Wilson, Van Halbeek (bib1) 1989; 264 Xia, Wang, Lin, Wang, Chu, Zhuang, Zhang (bib40) 2016 Liu, Yi, Zhuang, Zhang (bib36) 2015; 204 Xu, Lin, Mi, Pang, Wang (bib39) 2023; 107 Cole (bib44) 2012; 10 De Medeiros, Norman (bib8) 2009; 15 Morgan, Birken, Canfield (bib21) 1975; 250 Wiren, Potts, Kronenberg (bib32) 1988; 263 Nwabuobi, Arlier, Schatz, Guzeloglu-Kayisli, Lockwood, Kayisli (bib11) 2017; 18 Baik, Dahodwala, Oduah, Talman, Gemmill, Gasimli, Datta, Yang, Li, Zhang (bib38) 2015; 10 Butler, Spearman (bib46) 2014; 30 Petraglia, Serour, Chapron (bib15) 2013; 123 Recanati, Coca-Whiteford, Scheidl, Sissolak, Jungbauer (bib41) 2022; 118 Rajendra, Peery, Barnard (bib27) 2016; 32 Knappskog, Ravneberg, Gjerdrum, Troβe, Stern, Pryme (bib31) 2007; 128 Koistinen, Koel, Peters, Rinken, Lundin, Tuuri, Tapanainen, Alfthan, Salumets, Stenman (bib45) 2019; 479 Filicori, Fazleabas, Huhtaniemi, Licht, Rao, Tesarik, Zygmunt (bib12) 2005; 84 Heum, Chul, Seok, Hee, Bae, Choon (bib42) 2005; 15 Hugues (bib14) 2004; 3 Zygmunt, Herr, Keller-Schoenwetter, Kunzi-Rapp, Munstedt, Rao, Lang, Preissner (bib17) 2002; 87 Defaus, Gupta, Andreu, Gutierrez-Gallego (bib47) 2014; 139 de Lima, Lanza (bib23) 2021; 13 O'Flaherty, Bergin, Flampouri, Mota, Obaidi, Quigley, Xie, Butler (bib5) 2020; 43 Stern, Olsen, Tröße, Ravneberg, Pryme (bib28) 2007; 2 Petraglia (10.1016/j.pep.2024.106596_bib15) 2013; 123 Defaus (10.1016/j.pep.2024.106596_bib47) 2014; 139 Lin (10.1016/j.pep.2024.106596_bib24) 2017; 12 Xu (10.1016/j.pep.2024.106596_bib39) 2023; 107 Attallah (10.1016/j.pep.2024.106596_bib30) 2017; 132 De Medeiros (10.1016/j.pep.2024.106596_bib8) 2009; 15 Spellman (10.1016/j.pep.2024.106596_bib1) 1989; 264 Schjoldager (10.1016/j.pep.2024.106596_bib10) 2020; 21 Rajendra (10.1016/j.pep.2024.106596_bib27) 2016; 32 Gupta (10.1016/j.pep.2024.106596_bib37) 1999; 22 Xia (10.1016/j.pep.2024.106596_bib40) 2016 Majumdar (10.1016/j.pep.2024.106596_bib16) 2019; 12 Zhang (10.1016/j.pep.2024.106596_bib7) 2010 Alves (10.1016/j.pep.2024.106596_bib18) 2017 de Lima (10.1016/j.pep.2024.106596_bib23) 2021; 13 Filicori (10.1016/j.pep.2024.106596_bib12) 2005; 84 Zygmunt (10.1016/j.pep.2024.106596_bib17) 2002; 87 Nwabuobi (10.1016/j.pep.2024.106596_bib11) 2017; 18 Wiren (10.1016/j.pep.2024.106596_bib32) 1988; 263 Kim (10.1016/j.pep.2024.106596_bib3) 2012; 93 Hugues (10.1016/j.pep.2024.106596_bib14) 2004; 3 Zhang (10.1016/j.pep.2024.106596_bib33) 2005; 7 Zhu (10.1016/j.pep.2024.106596_bib6) 2012; 30 Stramaglia (10.1016/j.pep.2024.106596_bib19) 2008 Fraietta (10.1016/j.pep.2024.106596_bib13) 2013; 68 Chen (10.1016/j.pep.2024.106596_bib34) 2016; 118 Cho (10.1016/j.pep.2024.106596_bib22) 2019 O'Flaherty (10.1016/j.pep.2024.106596_bib5) 2020; 43 Recanati (10.1016/j.pep.2024.106596_bib41) 2022; 118 Kantardjieff (10.1016/j.pep.2024.106596_bib2) 2014 Ramezani (10.1016/j.pep.2024.106596_bib29) 2017; 135 Cole (10.1016/j.pep.2024.106596_bib44) 2012; 10 Butler (10.1016/j.pep.2024.106596_bib46) 2014; 30 Morgan (10.1016/j.pep.2024.106596_bib21) 1975; 250 Wang (10.1016/j.pep.2024.106596_bib48) 2017 Knappskog (10.1016/j.pep.2024.106596_bib31) 2007; 128 Fournier (10.1016/j.pep.2024.106596_bib9) 2016 Baik (10.1016/j.pep.2024.106596_bib38) 2015; 10 Cumming (10.1016/j.pep.2024.106596_bib43) 2003; 38 Peng (10.1016/j.pep.2024.106596_bib35) 2016; 7 Urli (10.1016/j.pep.2024.106596_bib4) 2015 Kober (10.1016/j.pep.2024.106596_bib20) 2013; 110 Inouye (10.1016/j.pep.2024.106596_bib25) 2015; 109 Liu (10.1016/j.pep.2024.106596_bib36) 2015; 204 Heum (10.1016/j.pep.2024.106596_bib42) 2005; 15 Ye (10.1016/j.pep.2024.106596_bib26) 2010; 26 Stern (10.1016/j.pep.2024.106596_bib28) 2007; 2 Koistinen (10.1016/j.pep.2024.106596_bib45) 2019; 479 |
| References_xml | – start-page: 35 year: 2015 ident: bib4 article-title: High productivity, serum-free, suspension CHO cell culture process development for anticancer therapeutic protein publication-title: JOSHUA – volume: 109 start-page: 47 year: 2015 end-page: 54 ident: bib25 article-title: Codon optimization of genes for efficient protein expression in mammalian cells by selection of only preferred human codons publication-title: Protein Expr. Purif. – volume: 12 start-page: 53 year: 2019 end-page: 58 ident: bib16 article-title: A multicenter, randomized, equivalence trial of a new recombinant human chorionic gonadotropin preparation versus ovitrelle® for ovulation in women undergoing intrauterine insemination following ovarian stimulation publication-title: J. Hum. Reprod. Sci. – volume: 30 start-page: 1158 year: 2012 end-page: 1170 ident: bib6 article-title: Mammalian cell protein expression for biopharmaceutical production publication-title: Biotechnol. Adv. – volume: 15 start-page: 69 year: 2009 end-page: 95 ident: bib8 article-title: Human choriogonadotrophin protein core and sugar branches heterogeneity: basic and clinical insights publication-title: Hum. Reprod. Update – start-page: 1 year: 2017 end-page: 23 ident: bib18 article-title: Strategies and considerations for improving expression of “difficult to express” proteins in CHO cells publication-title: Heterologous Protein Production in CHO Cells: Methods and Protocols – volume: 132 start-page: 27 year: 2017 end-page: 33 ident: bib30 article-title: A highly efficient modified human serum albumin signal peptide to secrete proteins in cells derived from different mammalian species publication-title: Protein Expr. Purif. – volume: 22 start-page: 273 year: 1999 end-page: 283 ident: bib37 article-title: Hyperexpression of biologically active human chorionic gonadotropin using the methylotropic yeast, Pichia pastoris publication-title: J. Mol. Endocrinol. – volume: 18 start-page: 2037 year: 2017 ident: bib11 article-title: hCG: biological functions and clinical applications publication-title: Int. J. Mol. Sci. – volume: 118 start-page: 145 year: 2022 end-page: 153 ident: bib41 article-title: Redissolution of recombinant antibodies precipitated by ZnCl2 publication-title: Process Biochem. – volume: 43 year: 2020 ident: bib5 article-title: Mammalian cell culture for production of recombinant proteins: a review of the critical steps in their biomanufacturing publication-title: Biotechnol. Adv. – volume: 250 start-page: 5247 year: 1975 end-page: 5258 ident: bib21 article-title: The amino acid sequence of human chorionic gonadotropin. The alpha subunit and beta subunit publication-title: J. Biol. Chem. – volume: 26 start-page: 1431 year: 2010 end-page: 1437 ident: bib26 article-title: Rapid protein production using CHO stable transfection pools publication-title: Biotechnol. Prog. – start-page: 25 year: 2017 end-page: 44 ident: bib48 article-title: Glycoengineering of CHO cells to improve product quality publication-title: Heterologous Protein Production in CHO Cells: Methods and Protocols – volume: 12 year: 2017 ident: bib24 article-title: Impact of signal peptides on Furin‐2A mediated monoclonal antibody secretion in CHO cells publication-title: Biotechnol. J. – volume: 128 start-page: 705 year: 2007 end-page: 715 ident: bib31 article-title: The level of synthesis and secretion of Gaussia princeps luciferase in transfected CHO cells is heavily dependent on the choice of signal peptide publication-title: J. Biotechnol. – volume: 7 start-page: 189 year: 2016 end-page: 197 ident: bib35 article-title: Enhanced recombinant factor VII expression in Chinese hamster ovary cells by optimizing signal peptides and fed-batch medium publication-title: Bioengineered – volume: 107 start-page: 1063 year: 2023 end-page: 1075 ident: bib39 article-title: Progress in fed-batch culture for recombinant protein production in CHO cells publication-title: Appl. Microbiol. Biotechnol. – volume: 10 start-page: 1067 year: 2015 end-page: 1081 ident: bib38 article-title: Optimization of bioprocess conditions improves production of a CHO cell‐derived, bioengineered heparin publication-title: Biotechnol. J. – year: 2014 ident: bib2 article-title: Mammalian Cell Cultures for Biologics Manufacturing – volume: 21 start-page: 729 year: 2020 end-page: 749 ident: bib10 article-title: Global view of human protein glycosylation pathways and functions publication-title: Nat. Rev. Mol. Cell Biol. – volume: 10 start-page: 1 year: 2012 end-page: 18 ident: bib44 article-title: hCG, the wonder of today's science publication-title: Reprod. Biol. Endocrinol. – volume: 135 start-page: 24 year: 2017 end-page: 32 ident: bib29 article-title: Improving Pertuzumab production by gene optimization and proper signal peptide selection publication-title: Protein Expr. Purif. – volume: 479 start-page: 103 year: 2019 end-page: 109 ident: bib45 article-title: Hyperglycosylated hCG activates LH/hCG-receptor with lower activity than hCG publication-title: Mol. Cell. Endocrinol. – volume: 87 start-page: 5290 year: 2002 end-page: 5296 ident: bib17 article-title: Characterization of human chorionic gonadotropin as a novel angiogenic factor publication-title: J. Clin. Endocrinol. Metabol. – volume: 84 start-page: 275 year: 2005 end-page: 284 ident: bib12 article-title: Novel concepts of human chorionic gonadotropin: reproductive system interactions and potential in the management of infertility publication-title: Fertil. Steril. – volume: 123 start-page: S4 year: 2013 end-page: S8 ident: bib15 article-title: The changing prevalence of infertility publication-title: Int. J. Gynecol. Obstet. – volume: 15 start-page: 395 year: 2005 end-page: 402 ident: bib42 article-title: Purification and characterization of recombinant human follicle stimulating hormone produced by Chinese hamster ovary cells publication-title: J. Microbiol. Biotechnol. – volume: 3 start-page: 371 year: 2004 end-page: 379 ident: bib14 article-title: Comparative use of urinary and recombinant human chorionic gonadotropins in women publication-title: Treat. Endocrinol. – year: 2008 ident: bib19 article-title: Improving protein production in CHO cells publication-title: BioPharm Int. 2008 – volume: 32 start-page: 1301 year: 2016 end-page: 1307 ident: bib27 article-title: Generation of stable Chinese hamster ovary pools yielding antibody titers of up to 7.6 g/L using the piggyBac transposon system publication-title: Biotechnol. Prog. – volume: 263 start-page: 19771 year: 1988 end-page: 19777 ident: bib32 article-title: Importance of the propeptide sequence of human preproparathyroid hormone for signal sequence function publication-title: J. Biol. Chem. – volume: 264 start-page: 14100 year: 1989 end-page: 14111 ident: bib1 article-title: Carbohydrate structures of human tissue plasminogen activator expressed in Chinese hamster ovary cells publication-title: J. Biol. Chem. – volume: 110 start-page: 1164 year: 2013 end-page: 1173 ident: bib20 article-title: Optimized signal peptides for the development of high expressing CHO cell lines publication-title: Biotechnol. Bioeng. – start-page: 75 year: 2016 end-page: 81 ident: bib9 publication-title: Human Chorionic Gonadotropin: Different Glycoforms and Biological Activity Depending on its Source of Production – volume: 139 start-page: 2944 year: 2014 end-page: 2967 ident: bib47 article-title: Mammalian protein glycosylation–structure versus function publication-title: Analyst – volume: 2 start-page: 1 year: 2007 end-page: 17 ident: bib28 article-title: Improving mammalian cell factories: the selection of signal peptide has a major impact on recombinant protein synthesis and secretion in mammalian cells publication-title: Trends Cell Mol. Biol. – start-page: 157 year: 2010 end-page: 178 ident: bib7 article-title: Mammalian cell culture for biopharmaceutical production publication-title: Manual Industrial Microbio. Biotechnol. – start-page: 137 year: 2016 end-page: 151 ident: bib40 article-title: Advances and practices of bioprocess scale-up publication-title: Bioreactor Engineering Research and Industrial Applications II – volume: 38 start-page: 433 year: 2003 end-page: 455 ident: bib43 article-title: Pathways and functions of mammalian protein glycosylation publication-title: N. Compr. Biochem. – volume: 13 start-page: 2160 year: 2021 ident: bib23 article-title: 2A and 2A-like sequences: distribution in different virus species and applications in biotechnology publication-title: Viruses – volume: 68 start-page: 81 year: 2013 end-page: 88 ident: bib13 article-title: Hypogonadotropic hypogonadism revisited publication-title: Clinics – volume: 93 start-page: 917 year: 2012 end-page: 930 ident: bib3 article-title: CHO cells in biotechnology for production of recombinant proteins: current state and further potential publication-title: Appl. Microbiol. Biotechnol. – volume: 7 start-page: 354 year: 2005 end-page: 365 ident: bib33 article-title: Alteration in the IL‐2 signal peptide affects secretion of proteins in vitro and in vivo publication-title: J. Gene Med.: A cross‐disciplinary journal for research on the science of gene transfer and its clinical applications – volume: 118 start-page: 105 year: 2016 end-page: 112 ident: bib34 article-title: High-efficiency secretory expression of human neutrophil gelatinase-associated lipocalin from mammalian cell lines with human serum albumin signal peptide publication-title: Protein Expr. Purif. – volume: 204 start-page: 63 year: 2015 end-page: 69 ident: bib36 article-title: Limitations in the process of transcription and translation inhibit recombinant human chorionic gonadotropin expression in CHO cells publication-title: J. Biotechnol. – year: 2019 ident: bib22 publication-title: Efficient Interleukin-21 Production by Optimization of Codon and Signal Peptide in Chinese Hamster Ovarian Cells – volume: 30 start-page: 107 year: 2014 end-page: 112 ident: bib46 article-title: The choice of mammalian cell host and possibilities for glycosylation engineering publication-title: Curr. Opin. Biotechnol. – volume: 118 start-page: 145 year: 2022 ident: 10.1016/j.pep.2024.106596_bib41 article-title: Redissolution of recombinant antibodies precipitated by ZnCl2 publication-title: Process Biochem. doi: 10.1016/j.procbio.2022.04.023 – volume: 123 start-page: S4 year: 2013 ident: 10.1016/j.pep.2024.106596_bib15 article-title: The changing prevalence of infertility publication-title: Int. J. Gynecol. Obstet. doi: 10.1016/j.ijgo.2013.09.005 – volume: 12 year: 2017 ident: 10.1016/j.pep.2024.106596_bib24 article-title: Impact of signal peptides on Furin‐2A mediated monoclonal antibody secretion in CHO cells publication-title: Biotechnol. J. doi: 10.1002/biot.201700268 – volume: 43 year: 2020 ident: 10.1016/j.pep.2024.106596_bib5 article-title: Mammalian cell culture for production of recombinant proteins: a review of the critical steps in their biomanufacturing publication-title: Biotechnol. Adv. – volume: 15 start-page: 69 year: 2009 ident: 10.1016/j.pep.2024.106596_bib8 article-title: Human choriogonadotrophin protein core and sugar branches heterogeneity: basic and clinical insights publication-title: Hum. Reprod. Update doi: 10.1093/humupd/dmn036 – volume: 135 start-page: 24 year: 2017 ident: 10.1016/j.pep.2024.106596_bib29 article-title: Improving Pertuzumab production by gene optimization and proper signal peptide selection publication-title: Protein Expr. Purif. doi: 10.1016/j.pep.2017.04.013 – volume: 204 start-page: 63 year: 2015 ident: 10.1016/j.pep.2024.106596_bib36 article-title: Limitations in the process of transcription and translation inhibit recombinant human chorionic gonadotropin expression in CHO cells publication-title: J. Biotechnol. doi: 10.1016/j.jbiotec.2014.12.005 – volume: 12 start-page: 53 year: 2019 ident: 10.1016/j.pep.2024.106596_bib16 article-title: A multicenter, randomized, equivalence trial of a new recombinant human chorionic gonadotropin preparation versus ovitrelle® for ovulation in women undergoing intrauterine insemination following ovarian stimulation publication-title: J. Hum. Reprod. Sci. doi: 10.4103/jhrs.JHRS_101_18 – volume: 10 start-page: 1067 year: 2015 ident: 10.1016/j.pep.2024.106596_bib38 article-title: Optimization of bioprocess conditions improves production of a CHO cell‐derived, bioengineered heparin publication-title: Biotechnol. J. doi: 10.1002/biot.201400665 – volume: 264 start-page: 14100 year: 1989 ident: 10.1016/j.pep.2024.106596_bib1 article-title: Carbohydrate structures of human tissue plasminogen activator expressed in Chinese hamster ovary cells publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)71649-9 – volume: 18 start-page: 2037 year: 2017 ident: 10.1016/j.pep.2024.106596_bib11 article-title: hCG: biological functions and clinical applications publication-title: Int. J. Mol. Sci. doi: 10.3390/ijms18102037 – start-page: 1 year: 2017 ident: 10.1016/j.pep.2024.106596_bib18 article-title: Strategies and considerations for improving expression of “difficult to express” proteins in CHO cells – volume: 118 start-page: 105 year: 2016 ident: 10.1016/j.pep.2024.106596_bib34 article-title: High-efficiency secretory expression of human neutrophil gelatinase-associated lipocalin from mammalian cell lines with human serum albumin signal peptide publication-title: Protein Expr. Purif. doi: 10.1016/j.pep.2015.10.012 – volume: 13 start-page: 2160 year: 2021 ident: 10.1016/j.pep.2024.106596_bib23 article-title: 2A and 2A-like sequences: distribution in different virus species and applications in biotechnology publication-title: Viruses doi: 10.3390/v13112160 – volume: 22 start-page: 273 year: 1999 ident: 10.1016/j.pep.2024.106596_bib37 article-title: Hyperexpression of biologically active human chorionic gonadotropin using the methylotropic yeast, Pichia pastoris publication-title: J. Mol. Endocrinol. doi: 10.1677/jme.0.0220273 – volume: 10 start-page: 1 year: 2012 ident: 10.1016/j.pep.2024.106596_bib44 article-title: hCG, the wonder of today's science publication-title: Reprod. Biol. Endocrinol. doi: 10.1186/1477-7827-10-24 – start-page: 137 year: 2016 ident: 10.1016/j.pep.2024.106596_bib40 article-title: Advances and practices of bioprocess scale-up – volume: 93 start-page: 917 year: 2012 ident: 10.1016/j.pep.2024.106596_bib3 article-title: CHO cells in biotechnology for production of recombinant proteins: current state and further potential publication-title: Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-011-3758-5 – volume: 30 start-page: 1158 year: 2012 ident: 10.1016/j.pep.2024.106596_bib6 article-title: Mammalian cell protein expression for biopharmaceutical production publication-title: Biotechnol. Adv. doi: 10.1016/j.biotechadv.2011.08.022 – volume: 109 start-page: 47 year: 2015 ident: 10.1016/j.pep.2024.106596_bib25 article-title: Codon optimization of genes for efficient protein expression in mammalian cells by selection of only preferred human codons publication-title: Protein Expr. Purif. doi: 10.1016/j.pep.2015.02.002 – volume: 2 start-page: 1 year: 2007 ident: 10.1016/j.pep.2024.106596_bib28 article-title: Improving mammalian cell factories: the selection of signal peptide has a major impact on recombinant protein synthesis and secretion in mammalian cells publication-title: Trends Cell Mol. Biol. – volume: 7 start-page: 189 year: 2016 ident: 10.1016/j.pep.2024.106596_bib35 article-title: Enhanced recombinant factor VII expression in Chinese hamster ovary cells by optimizing signal peptides and fed-batch medium publication-title: Bioengineered doi: 10.1080/21655979.2016.1176656 – volume: 479 start-page: 103 year: 2019 ident: 10.1016/j.pep.2024.106596_bib45 article-title: Hyperglycosylated hCG activates LH/hCG-receptor with lower activity than hCG publication-title: Mol. Cell. Endocrinol. doi: 10.1016/j.mce.2018.09.006 – volume: 250 start-page: 5247 year: 1975 ident: 10.1016/j.pep.2024.106596_bib21 article-title: The amino acid sequence of human chorionic gonadotropin. The alpha subunit and beta subunit publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)41303-3 – volume: 68 start-page: 81 year: 2013 ident: 10.1016/j.pep.2024.106596_bib13 article-title: Hypogonadotropic hypogonadism revisited publication-title: Clinics doi: 10.6061/clinics/2013(Sup01)09 – volume: 26 start-page: 1431 year: 2010 ident: 10.1016/j.pep.2024.106596_bib26 article-title: Rapid protein production using CHO stable transfection pools publication-title: Biotechnol. Prog. doi: 10.1002/btpr.469 – volume: 7 start-page: 354 year: 2005 ident: 10.1016/j.pep.2024.106596_bib33 article-title: Alteration in the IL‐2 signal peptide affects secretion of proteins in vitro and in vivo publication-title: J. Gene Med.: A cross‐disciplinary journal for research on the science of gene transfer and its clinical applications doi: 10.1002/jgm.677 – volume: 139 start-page: 2944 year: 2014 ident: 10.1016/j.pep.2024.106596_bib47 article-title: Mammalian protein glycosylation–structure versus function publication-title: Analyst doi: 10.1039/C3AN02245E – year: 2019 ident: 10.1016/j.pep.2024.106596_bib22 – start-page: 157 year: 2010 ident: 10.1016/j.pep.2024.106596_bib7 article-title: Mammalian cell culture for biopharmaceutical production publication-title: Manual Industrial Microbio. Biotechnol. – year: 2014 ident: 10.1016/j.pep.2024.106596_bib2 – volume: 30 start-page: 107 year: 2014 ident: 10.1016/j.pep.2024.106596_bib46 article-title: The choice of mammalian cell host and possibilities for glycosylation engineering publication-title: Curr. Opin. Biotechnol. doi: 10.1016/j.copbio.2014.06.010 – volume: 3 start-page: 371 year: 2004 ident: 10.1016/j.pep.2024.106596_bib14 article-title: Comparative use of urinary and recombinant human chorionic gonadotropins in women publication-title: Treat. Endocrinol. doi: 10.2165/00024677-200403060-00005 – volume: 132 start-page: 27 year: 2017 ident: 10.1016/j.pep.2024.106596_bib30 article-title: A highly efficient modified human serum albumin signal peptide to secrete proteins in cells derived from different mammalian species publication-title: Protein Expr. Purif. doi: 10.1016/j.pep.2017.01.003 – volume: 107 start-page: 1063 year: 2023 ident: 10.1016/j.pep.2024.106596_bib39 article-title: Progress in fed-batch culture for recombinant protein production in CHO cells publication-title: Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-022-12342-x – volume: 110 start-page: 1164 year: 2013 ident: 10.1016/j.pep.2024.106596_bib20 article-title: Optimized signal peptides for the development of high expressing CHO cell lines publication-title: Biotechnol. Bioeng. doi: 10.1002/bit.24776 – year: 2008 ident: 10.1016/j.pep.2024.106596_bib19 article-title: Improving protein production in CHO cells publication-title: BioPharm Int. 2008 – volume: 87 start-page: 5290 year: 2002 ident: 10.1016/j.pep.2024.106596_bib17 article-title: Characterization of human chorionic gonadotropin as a novel angiogenic factor publication-title: J. Clin. Endocrinol. Metabol. doi: 10.1210/jc.2002-020642 – volume: 263 start-page: 19771 year: 1988 ident: 10.1016/j.pep.2024.106596_bib32 article-title: Importance of the propeptide sequence of human preproparathyroid hormone for signal sequence function publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)77701-1 – volume: 128 start-page: 705 year: 2007 ident: 10.1016/j.pep.2024.106596_bib31 article-title: The level of synthesis and secretion of Gaussia princeps luciferase in transfected CHO cells is heavily dependent on the choice of signal peptide publication-title: J. Biotechnol. doi: 10.1016/j.jbiotec.2006.11.026 – start-page: 35 year: 2015 ident: 10.1016/j.pep.2024.106596_bib4 article-title: High productivity, serum-free, suspension CHO cell culture process development for anticancer therapeutic protein publication-title: JOSHUA – volume: 38 start-page: 433 year: 2003 ident: 10.1016/j.pep.2024.106596_bib43 article-title: Pathways and functions of mammalian protein glycosylation publication-title: N. Compr. Biochem. doi: 10.1016/S0167-7306(03)38026-3 – start-page: 75 year: 2016 ident: 10.1016/j.pep.2024.106596_bib9 – volume: 21 start-page: 729 year: 2020 ident: 10.1016/j.pep.2024.106596_bib10 article-title: Global view of human protein glycosylation pathways and functions publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/s41580-020-00294-x – volume: 32 start-page: 1301 year: 2016 ident: 10.1016/j.pep.2024.106596_bib27 article-title: Generation of stable Chinese hamster ovary pools yielding antibody titers of up to 7.6 g/L using the piggyBac transposon system publication-title: Biotechnol. Prog. doi: 10.1002/btpr.2307 – volume: 84 start-page: 275 year: 2005 ident: 10.1016/j.pep.2024.106596_bib12 article-title: Novel concepts of human chorionic gonadotropin: reproductive system interactions and potential in the management of infertility publication-title: Fertil. Steril. doi: 10.1016/j.fertnstert.2005.02.033 – volume: 15 start-page: 395 year: 2005 ident: 10.1016/j.pep.2024.106596_bib42 article-title: Purification and characterization of recombinant human follicle stimulating hormone produced by Chinese hamster ovary cells publication-title: J. Microbiol. Biotechnol. – start-page: 25 year: 2017 ident: 10.1016/j.pep.2024.106596_bib48 article-title: Glycoengineering of CHO cells to improve product quality publication-title: Heterologous Protein Production in CHO Cells: Methods and Protocols doi: 10.1007/978-1-4939-6972-2_2 |
| SSID | ssj0011605 |
| Score | 2.432733 |
| Snippet | Optimizations of the gene expression cassette combined with the selection of an appropriate signal peptide are important factors that must be considered to... |
| SourceID | proquest pubmed crossref elsevier |
| SourceType | Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | 106596 |
| SubjectTerms | Animals CHO Cells Chorionic Gonadotropin - biosynthesis Chorionic Gonadotropin - genetics Chorionic Gonadotropin - pharmacology Cricetinae Cricetulus Gene Expression Human chorionic gonadotropin Humans Protein Sorting Signals - genetics Recombinant Proteins - biosynthesis Recombinant Proteins - genetics Signal peptide Stable pool. bioprocess optimization Transfection |
| Title | Strategies for improving expression of recombinant human chorionic gonadotropin in Chinese Hamster Ovary (CHO) cells |
| URI | https://dx.doi.org/10.1016/j.pep.2024.106596 https://www.ncbi.nlm.nih.gov/pubmed/39218246 https://www.proquest.com/docview/3099856234 |
| Volume | 225 |
| WOSCitedRecordID | wos001306816900001&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| journalDatabaseRights | – providerCode: PRVESC databaseName: ScienceDirect Freedom Collection customDbUrl: eissn: 1096-0279 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0011605 issn: 1046-5928 databaseCode: AIEXJ dateStart: 19950201 isFulltext: true titleUrlDefault: https://www.sciencedirect.com providerName: Elsevier |
| link | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1bb9MwFLa6DcFeEGzAymUyEkLAlCmJ3Vweu2moQ2jbw5D6FtmpQ9utSZU2Vbefwy_l-JaGQSd4QKqiNBenyvfVPveD0DsSwCLkMd_hwhMOJRz2wgF3ggB0MckBnqqS-V_Ds7Oo348vWq0fNhdmcR3mebRcxtP_CjUcA7Bl6uw_wF0PCgdgH0CHLcAO278C3tabFarSgkyDNFYDsTRBr0pClJrwhKs4GNOoDybCcqQa4nwH8Ry01VImU6m0wKFqVHnQYxNZV-HgfCFj7aT_t3cuzQrS-j9rirkXsvrDKG8-UhUkqEoZmfSL8_-oqK6YTnc_HQq-cgBVZVFpm_VkxBpX37JbnRxflDOW1RrBDL6MnCORXw0ZrNNqApN7Y9Y0bPidhmFD6MnYVQHSutmMna19v9OYbz3pFg7-uBRoq8T4cCpkWVKfHv5-LQA3nSgagJQIiha9U5RbL_Pm1Aba8sNODDPnVvf0pP-l9lV5oBFaf7mKHLzzxG300I6xTvhZp9woIefyCXpstBPc1ax6iloi30G73ZzNi8kNfo9VvLByxOygR8e2V-Aumq9Ih4F0uCYdXjEAFxlukA4r0uGadLhJOgwfQzpsSIcV6fAHoNxHrAj3DH37fHJ53HNMPw8nJR0yd4gA7V94Hmck8zrMFWkogpimoJL4QRRHnPgC1pTAHfCQy6RontJBxrKAiYhTOiDP0WZe5GIPYQY0cGMixXFKfVew0Et9GJlGJAOZNG0j177oJDXF7mXPlevERjWOE4ApkTAlGqY2-lTfMtWVXu67mFr0EiOqahE0Afrdd9tbi3QCCMmXxXJRVLOEgKYWSV2EttELTYH6V1j2vFx75hXaXv2DXqPNeVmJN-hBupiPZuU-2gj70b6h7U9JTMU8 |
| linkProvider | Elsevier |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Strategies+for+improving+expression+of+recombinant+human+chorionic+gonadotropin+in+Chinese+Hamster+Ovary+%28CHO%29+cells&rft.jtitle=Protein+expression+and+purification&rft.au=Boukari%2C+Iheb&rft.au=Rourou%2C+Samia&rft.au=Bouzazi%2C+Dorsaf&rft.au=Essafi-Benkhadir%2C+Khadija&rft.date=2025-01-01&rft.eissn=1096-0279&rft.volume=225&rft.spage=106596&rft_id=info:doi/10.1016%2Fj.pep.2024.106596&rft_id=info%3Apmid%2F39218246&rft.externalDocID=39218246 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1046-5928&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1046-5928&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1046-5928&client=summon |