Protein expression and purification最新文献

{"title":"The superiority of MabSelect VL, Cytiva's second-generation Protein L resin, over three other affinity resins in purifying a VHH-containing trispecific antibody","authors":"Ruomei Lv ,&nbsp;Wenjing Qi ,&nbsp;Yifeng Li","doi":"10.1016/j.pep.2025.106873","DOIUrl":"10.1016/j.pep.2025.106873","url":null,"abstract":"<div><div>Affinity chromatography is widely utilized for initial product capture in antibody purification. Besides Protein A resins, other affinity resins that bind different subdomains of an antibody have also been developed. For example, Protein L resin, KappaSelect, LambdaFabSelect and Praesto 70 CH1 selectively bind the variable region of kappa light chain (LC), constant region of kappa LC, constant region of lambda LC and CH1 domain of the heavy chain (HC), respectively. Affinity media with distinct specificities provide more options for antibody purification. For a given bispecific antibody (bsAb) purification case, depending on the composition difference between the product and byproducts, one affinity resin may outperform the others for byproduct removal. In the current study, we compared four affinity resins, Praesto Jetted A50 (a Protein A resin), Praesto 70 CH1, KappaSelect and MabSelect VL (Cytiva's second-generation Protein L resin), for their effectiveness in removing byproducts associated with a VHH-containing trispecific antibody (TsAb). The data suggested that the three non-Protein A resins outperformed the Protein A resin for byproduct removal. Among the three non-Protein A resins, MabSelect VL provided the best byproduct clearance, and it removed half-antibody, homodimers and most aggregates. This work reconfirms the necessity of screening different affinity resins with distinct specificities for achieving the best separation.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106873"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145794505","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Extraction and characterization of functional duckweed proteins using alkaline, enzymatic, and ultrasound-assisted techniques","authors":"Ayça Akyüz,&nbsp;Seda Ersus","doi":"10.1016/j.pep.2025.106860","DOIUrl":"10.1016/j.pep.2025.106860","url":null,"abstract":"<div><div>The urgent need for sustainable, plant-based protein sources has brought aquatic crops like duckweed (Lemnaceae) into focus due to their high protein content, fast growth, and minimal resource requirements. This study aims to optimize and compare alkaline, enzyme-assisted, and ultrasound-assisted extraction techniques to produce high-yield, functional protein concentrates from <em>Lemna minor</em>. Key extraction parameters—pH, temperature, and solvent-to-solid ratio—were systematically optimized, identifying pH 9, 55 °C, and 5 mL/g as ideal conditions. Ultrasound treatment (100 % amplitude, 10 min) and Alcalase L enzyme application significantly enhanced protein yields. Ultrasound-assisted extraction proved most effective, increasing protein yield by more than fivefold compared to conventional alkaline methods, reaching 60.09 % protein content on a dry basis. The resulting protein concentrates displayed desirable functional properties, including excellent solubility (92.19 % at pH 9), foaming capacity (92.62 %), and emulsion activity, all of which are critical for food applications. Comprehensive structural and compositional analyses confirmed the presence of essential amino acids, high mineral content (notably calcium and phosphorus), and acceptable techno-functional behavior. SEM and FTIR analyses supported the structural integrity of the extracted proteins, while flowability assessments suggested suitability for powder-based formulations. This research demonstrates that ultrasound-assisted protein isolation from duckweed offers a scalable and efficient strategy for producing high-quality protein concentrates. These findings position duckweed as a promising, sustainable protein source with strong potential for incorporation into functional foods and novel plant-based formulations.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106860"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145557593","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Comparative biophysical and functional analysis of TCZ-UFRJ, a potential biosimilar to Actemra","authors":"Sanclayver Corrêa Araújo ,&nbsp;Federico Francisco Marsili ,&nbsp;Renata Guimarães Alvim ,&nbsp;Katia Maria dos Santos Cabral ,&nbsp;Heitor Affonso de Paula Neto ,&nbsp;Yraima Cordeiro ,&nbsp;Marcius da Silva Almeida ,&nbsp;Leda dos Reis Castilho ,&nbsp;Renato Sampaio Carvalho","doi":"10.1016/j.pep.2025.106841","DOIUrl":"10.1016/j.pep.2025.106841","url":null,"abstract":"<div><div>Biosimilar antibodies have become increasingly significant in the pharmaceutical market, driven by the expiration of patents on many reference products. This study presents a comparative analysis between the originator tocilizumab, used to treat inflammatory diseases such as rheumatoid arthritis, and the biosimilar candidate TCZ-UFRJ, produced in HEK293 cells. The investigation focused on various aspects, including primary, secondary, and tertiary structures, intact mass analysis, glycosylation pattern, and functional testing using the IL-6-sensitive THP-1 cell line and ligand binding assay. LC-MS peptide mapping achieved amino acid full sequence coverage for both TCZ-UFRJ and Actemra, confirming the identity of the biosimilar candidate. Both antibodies exhibited a similar secondary structure with a characteristic beta-sheet spectrum, as determined by circular dichroism. The intrinsic tryptophan emission fluorescence profile confirmed a correctly folded tertiary structure for both mAbs. Intact mass analysis demonstrated similar molecular mass and glycoform profiles. Glycosylation analysis revealed similar glycosylation sites and the presence of major N-glycans in both Actemra and TCZ-UFRJ. Dynamic light scattering analysis indicated a monodisperse sample without the presence of oligomers for both. An LSPR ligand binding assay confirmed the interaction between TCZ-UFRJ and the IL-6 receptor, demonstrating specific binding affinity. Subsequent functional testing in the IL-6-sensitive THP-1 cell line validated the biological activity of TCZ-UFRJ, supporting its potential as a biosimilar candidate. These preliminary findings suggest that TCZ-UFRJ holds promise as a biosimilar candidate to Actemra, but further comprehensive studies, including non-clinical and clinical trials, are essential to establish its safety, efficacy, and overall similarity to the originator drug.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106841"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145493275","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Optimized production and coagulation activity of rhFVII in HEK293 cells for bleeding disorders","authors":"Sen Zou ,&nbsp;Xiaoxiao Li ,&nbsp;Jiajun Liu ,&nbsp;Shuai Fan ,&nbsp;Zhaoyong Yang","doi":"10.1016/j.pep.2025.106867","DOIUrl":"10.1016/j.pep.2025.106867","url":null,"abstract":"<div><div>Hemophilia, a genetic disorder characterized by impaired blood clotting, necessitates innovative treatments. This study optimized the expression of recombinant human coagulation factor VII (rhFVII) in HEK293 cells to enhance its therapeutic efficacy. The human FVII gene was cloned into the pcDNA3.1 vector, and transient transfection was performed with an optimized DNA-to-PEI ratio (1:2) at 70 % cell density. Stable FVII-expressing cell lines were selected with G418, confirmed via RT-PCR, and adapted to suspension culture. rhFVII expression was analyzed using SDS-PAGE, Western blot, and ELISA, while its coagulation activity was evaluated by prothrombin time tests. Transient transfection yielded rhFVII concentrations of 10.22 μg/L and clotting activity of 232.46 %. Stable monoclonal HEK293 cells in suspension produced rhFVII at 11.22 mg/L with maximum coagulation activity of 563.17 % and high stability and safety. The findings underscore the successful optimization of rhFVII expression in HEK293 cells, paving the way for advancements in biopharmaceutical production and improved treatment options for bleeding disorders. Future research should focus on in vivo validation and further refinement of culture conditions to maximize protein yield and stability.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106867"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145687724","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"L-arginine interferes with functional studies of amyloid proteins","authors":"H.P. Chethana,&nbsp;U. Rathan Kumar,&nbsp;Gunimala Chakraborty,&nbsp;Arshdeep Sidhu","doi":"10.1016/j.pep.2025.106854","DOIUrl":"10.1016/j.pep.2025.106854","url":null,"abstract":"<div><div>Intrinsically disordered proteins/regions are abundant in cancer signalling pathways and neurodegenerative diseases like Parkinson's disease, amyotrophic lateral sclerosis, Alzheimer's disease, etc. Purification of intrinsically disordered proteins can be challenging due to their sticky nature. For intrinsically disordered amyloid proteins, in-vitro aggregation studies are ideal experiments to study their liquid to solid transition. However, over-expression of these proteins in <em>E. coli</em> often results in insoluble protein fraction that ends up in cell-pellet as inclusion bodies, on lysis and centrifugation. Supplementing purification buffers with l-arginine is known to increase the solubility of proteins. For most of the structured proteins increasing solubility translates into a higher yield of functional proteins. However, for aggregation prone proteins associated with neurodegenerative diseases, like α-synuclein (Parkinson's disease), Aβ (Alzheimer's disease), fused in sarcoma (amyotrophic lateral sclerosis), etc. inclusion of l-arginine might interfere with aggregation studies. To test our hypothesis, we purified aggregation prone α-synuclein and fused in sarcoma protein in the presence and absence of l-arginine and studied their fibrillization. While recombinant FUS is difficult to prepare, purification of α-synuclein is well established but in all the protocols a significant amount of protein remains as insoluble fraction in the pellet. Inclusion of l-arginine increases the yield of protein purification by about 3 folds for both the proteins, but the resulting protein does not aggregate into fibrils thus showing that increased solubility of amyloid proteins (α-synuclein and fused in sarcoma) in the presence of l-arginine is not suitable for aggregation studies.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106854"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145534691","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Expression and functional characterization of recombinant soluble CD40 Ligand in prokaryotic systems","authors":"Qi Xu ,&nbsp;Xinying He ,&nbsp;Jiale Bai ,&nbsp;Hanlin Liu ,&nbsp;Tao Hong ,&nbsp;Suying Dang ,&nbsp;Wei Zhang","doi":"10.1016/j.pep.2025.106874","DOIUrl":"10.1016/j.pep.2025.106874","url":null,"abstract":"<div><h3>Objective</h3><div>To develop an optimized prokaryotic expression system for producing functional soluble CD40 ligand (sCD40L) and characterize its hemostatic activity.</div></div><div><h3>Methods</h3><div>The codon-optimized <em>sCD40L</em> gene (encoding residues 113–261) was synthesized and cloned into pET28a vector via BamHI/XhoI sites. After transformation into <em>E. coli</em> BL21(DE3), soluble expression was induced with 0.5 mM IPTG at 20 °C for 12 h. The recombinant protein was purified using nickel-affinity chromatography and analyzed by SDS-PAGE and Western blot. Biological activity was assessed through in vitro platelet aggregation and in vivo hemostasis assays.</div></div><div><h3>Results</h3><div>The pET28a-sCD40L expression vector was successfully constructed, and the protein purity reached more than 90 %. Western blot confirmed the expected ∼20 kDa sCD40L. Functionally, the recombinant sCD40L enhanced platelet aggregation in a dose-dependent manner, and significantly reduced secondary bleeding time in mice.</div></div><div><h3>Conclusion</h3><div>Our optimized prokaryotic system efficiently produces functional sCD40L without requiring eukaryotic post-translational modifications, providing a valuable tool for studying CD40L-mediated hemostasis and developing potential therapeutic applications.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106874"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145786906","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Plasmid-transformed Bifidobacterium longum 105A secreting β-glucuronidase for prodrug conversion of SN-38 glucuronide","authors":"Atsushi Saisho ,&nbsp;Michiko Shimokawa ,&nbsp;Rintaro Kubo ,&nbsp;Yuri Enomoto ,&nbsp;Shun'ichiro Taniguchi ,&nbsp;Hiroaki Kobayashi","doi":"10.1016/j.pep.2025.106844","DOIUrl":"10.1016/j.pep.2025.106844","url":null,"abstract":"<div><div>The development of tumor-selective prodrug activation strategies remains a major challenge in cancer pharmacotherapy.</div><div>In this study, we focused on SN-38 glucuronide (SN-38G), a highly hydrophilic prodrug with low membrane permeability that remains pharmacologically inactive unless hydrolyzed by β-glucuronidase. To enable localized activation of SN-38G within tumors, we engineered a recombinant <em>Bifidobacterium longum</em> 105A strain capable of secreting β-glucuronidase. The enzyme was efficiently secreted under anaerobic conditions and retained stable catalytic activity in mildly acidic and hypoxic environments that resemble the tumor microenvironment. In an MTT assay using CT26 colon carcinoma cells, co-treatment with β-glucuronidase and SN-38G induced marked growth inhibition, whereas SN-38G alone showed no cytotoxic effect. Furthermore, HPLC analysis of culture supernatants confirmed enzymatic conversion of SN-38G into the active metabolite SN-38.</div><div>Together, these results provide a proof-of-concept for a microbial-enhanced prodrug activation approach in which plasmid-driven expression in <em>Bifidobacterium longum</em> 105A enables targeted release of SN-38. This strategy may contribute to the development of tumor-localized drug production systems capable of selectively activating diverse anticancer prodrugs with distinct mechanisms of action.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106844"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145493274","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Partial purification and characterization acidophilic lipase from Bacillus cereus ALP E1","authors":"Nindy Novita Sari ,&nbsp;Nurhasanah ,&nbsp;Titin Haryati","doi":"10.1016/j.pep.2025.106870","DOIUrl":"10.1016/j.pep.2025.106870","url":null,"abstract":"<div><div>The discovery of a new microbial lipase is crucial since its utilization has various industrial applications. <em>Bacillus cereus</em> is a strain that has emerged as a potential source of microbial lipase. Until now, the exploration of new lipases from <em>Bacillus cereus</em> remains limited. This study aims to obtain a lipase enzyme from <em>Bacillus cereus</em> ALP E1, as well as to purify and characterize the lipase produced by this strain. In this study, an extracellular acidophilic lipase from <em>Bacillus cereus</em> ALP E1 isolated from seawater at Panjang Port, Lampung, Indonesia was partially purified and characterized. Extracellular lipase was produced using submerged fermentation methods, and then partially purified with ammonium sulphate fractionation and dialysis. Partial purification successfully achieved a 12.31 purification fold with specific activity at 31083.14 U/mg. According to SDS-PAGE analysis, the purified lipase had a single dominant band estimated at 55 kDa. Lipase characterization revealed an optimal pH of 5, an optimal temperature of 40 °C, and the highest activity towards the substrate <em>p</em>-nitrophenyl stearate (C18). The lipase was activated by Ba²⁺ and deactivated by Mg²⁺. This lipase activity is enhanced by adding 1 % Tween 20, but it is deactivated by Tween 80. All tested organic solvents at 5 % concentration were able to activate the lipase with the optimized two-fold lipase activation using chloroform added. The results demonstrate that seawater is a promising source for discovering lipases with high activity. This complete characterization is important information and serves as a foundation for using lipase in appropriate industrial applications.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106870"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145725695","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Novel anti-NS1 human single domain antibody from dengue infected NS1 positive patients","authors":"Odedara Mitalben Bhikhabhai,&nbsp;Hemant Kumar","doi":"10.1016/j.pep.2025.106875","DOIUrl":"10.1016/j.pep.2025.106875","url":null,"abstract":"<div><div>Viruses of the flavivirus family significantly affect human health worldwide. Dengue virus (DENV), a member of the flavivirus family, causes pathogenic symptoms like high fever, severe headache and body pain upon infection. In some cases, it develops into severe dengue that is fatal. As a crucial pillar of immune response antibodies are produced against different epitopes of the dengue proteins and a collective response is generated by targeting critical proteins. A vaccine against dengue is still to be developed and new antibodies are the need of the hour. In our work we have isolated novel full length heavy chain variable region genes from peripheral blood mononuclear cell (PMBC) of NS1 positive DENV infected patients. The sequencing suggests that the isolated heavy chains to be novel and not yet reported. The sequence verified clones were sub cloned into expression vector pET-28a(+) for protein expression in <em>E. coli</em>. Selected heavy chains were overexpressed and purified to near homogeneity and further specific binding of purified heavy chain variable region with rNS1 was confirmed through competitive inhibition ELISA, dose dependent competitive inhibition ELISA and western blotting. ITC further confirmed the binding of rNS1 and SdAb3 with favourable free energy (ΔG = −9.22 kcal/mol). Identity of purified protein was confirmed by western blotting through anti-His antibody. It was found that a large amount of the purified protein was going in insoluble fraction and a protein refolding strategy was optimized with different buffer conditions. A buffer containing arginine, histidine and sucrose was found to be most efficient in solubilization of protein from insoluble fraction.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106875"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145850662","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Systematic optimization for high-level secretory expression of a thermostable zearalenone hydrolase ZENM in Pichia pastoris","authors":"Shida Zhao ,&nbsp;Qin Zhou ,&nbsp;Yuzhuo Wu ,&nbsp;Ying Hou ,&nbsp;Qi Wu ,&nbsp;Ding Li ,&nbsp;Jianhong Xu","doi":"10.1016/j.pep.2025.106843","DOIUrl":"10.1016/j.pep.2025.106843","url":null,"abstract":"<div><div>Zearalenone (ZEN), a mycotoxin commonly found in cereal grains, poses a significant threat to livestock health. ZEN hydrolase is considered a key tool for detoxifying ZEN contamination due to its high efficiency, cost-effectiveness, and ability to completely degrade the toxin. Among these enzymes, ZEN hydrolase ZENM is a promising candidate for industrial applications owing to its superior thermostability. In this study, ZENM was heterologously expressed in the <em>Pichia pastoris</em> system. The enzyme exhibited optimal activity at pH 8.0 and 60 °C, and maintained over 90 % of its relative activity within the 50–60 °C range. Its kinetic parameters, the apparent Michaelis-Menten constant (K_m, _app) and maximal reaction velocity (V_max), were determined to be 21.59 ± 7.34 μM and 0.031 ± 0.002 μM s⁻¹ mg⁻¹, respectively. The yield of ZENM was increased from 6.70 U/mL to 41.55 U/mL by utilizing the pre-Ost1-pro-α-factor signal peptide. Increasing the gene dosage further enhanced the yield to 50.87 U/mL. Furthermore, co-expression with molecular chaperones PDI and SEC12 elevated the yield to 72.29 U/mL and 68.88 U/mL, respectively. Ultimately, a 10.79-fold increase in ZENM production was achieved in shake flask cultures compared to the initial strain. This research establishes a solid foundation for advancing the industrial application of ZENM.</div></div>","PeriodicalId":20757,"journal":{"name":"Protein expression and purification","volume":"239 ","pages":"Article 106843"},"PeriodicalIF":1.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145615543","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}