Production of recombinant protein and polyclonal mouse antiserum for ferritin from Sipuncula Phascolosoma esculenta

Su, Xiurong; Du, Lili; Li, Yanyan; Li, Taiwu; Li, Dengfeng; Wang, Mengqian; He, Jingjing

doi:10.1016/j.fsi.2009.06.014

Cited by 11 publications

(10 citation statements)

References 18 publications

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“…IPTG was added to the log-phase bacterial culture at a final concentration of 1 mmol/liter to induce protein expression. The protein samples were analyzed using 12% SDS-PAGE ( Su et al . 2009 ).…”

Section: Methodsmentioning

confidence: 99%

Expression Profiles of the Heat Shock Protein 70 Gene in Response to Heat Stress in Agrotis c-nigrum (Lepidoptera: Noctuidae)

Yang

KuiJun

Han

2015

Journal of Insect Science

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Heat shock proteins (HSPs) are molecular chaperones, and their overexpression enhances the survivability and stress tolerance of the cell. To understand the characteristics of HSP70 in Agrotis c-nigrum Linnaeus larvae, the coding sequence of this protein was cloned, and the effect of heat stress on transcription and protein properties was assessed. The obtained cDNA sequence of HSP70 was 2,213 bp, which contained an ORF of 1,965 bp and encoded 654 amino acid residues. Isolated HSP70 cDNA demonstrated more than 80% identity with the sequences of other known insect HSP70s. Next, HSP70 was expressed in Escherichia coli BL21 (DE3) cells and identified using SDS-PAGE and western blotting analyses. In addition, anti-HSP70-specific antisera were prepared using a recombinant HSP70 protein, and the results showed that this antisera was very specific to AcHSP70. Real-time quantitative polymerase chain reaction detected the relative transcription of the HSP70 gene in larvae and the transcription of A. c-nigrum in response to high temperatures. Induction of HSP70 was up-regulated to peak expression at 36°C.

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Section: Methodsmentioning

confidence: 99%

Expression Profiles of the Heat Shock Protein 70 Gene in Response to Heat Stress in Agrotis c-nigrum (Lepidoptera: Noctuidae)

Yang

KuiJun

Han

2015

Journal of Insect Science

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“…IPTG was added to the log phase bacterial culture at the final concentration of 1 mmol/L to induce the protein expression. Protein samples were analyzed by 12% SDS-PAGE [12].…”

Section: Expression Of Hsp70 Proteinmentioning

confidence: 99%

Cloning and expression of HSP70 gene of sipuncula Phascolosoma esculenta

et al. 2010

Fish & Shellfish Immunology

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“…In this study, an attempt was made to investigate the ACE inhibitory activity of di-and tri-peptides derived from Phascolosoma esculenta, a marine deposit-feeding benthonic invertebrates, also a traditional seafood with over 70% protein (dry weight) in Southeast China [33,34]. Database of di-and tri-peptides derived from P. esculenta were established, and their ACE inhibitory activities were predicted by virtual hydrolysis and screening method.…”

Section: Introductionmentioning

confidence: 99%

Virtual screening for angiotensin I-converting enzyme inhibitory peptides from Phascolosoma esculenta

Zhang

Guo

et al. 2014

Bioresour. Bioprocess.

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Background: Many short peptides have proved to exhibit potential anti-hypertensive activity through the inhibition of the Angiotensin I-converting enzyme (ACE) activity and the regulation of blood pressure. However, the traditional experimental screening method for ACE inhibitory peptides is time consuming and costly, accompanied with the limitations as incomplete hydrolysis and peptides loss during purification process. Virtual methods with the aid of computer can break such bottle-neck of experimental work. In this study, an attempt was made to establish a library of di-and tri-peptides derived from proteins of Phascolosoma esculenta, a kind of seafood, through BIOPEP (http://www.uwm.edu.pl/biochemia/index.php/pl/biopep), and to screen highly active ACE inhibitory peptides by molecular docking with the help of LibDock module of Discovery Studio 3.5 software. Results: Two hundred and eighty four (284) di-and tri-peptides, derived from P. esculenta proteins after a virtual hydrolysis with pepsin, trypsin and a mixture of pepsin and trypsin, were predicted to possess ACE inhibitory activity, among which there are 99 ACE inhibitory peptides with estimated IC 50 less than 50 μM. Nine peptides were synthesized for the comparison between the estimated and the experimentally determined IC 50 . The results indicated that errors between the estimated and measured log(1/IC 50 ) are all less than 1.0 unit. Conclusions: Virtual method for peptide library construction and ACE inhibitory peptides screening efficiently demonstrated that P. esculenta proteins are prospect resource for food-origin ACE inhibitory peptide.

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Production of recombinant protein and polyclonal mouse antiserum for ferritin from Sipuncula Phascolosoma esculenta

Cited by 11 publications

References 18 publications

Expression Profiles of the Heat Shock Protein 70 Gene in Response to Heat Stress in Agrotis c-nigrum (Lepidoptera: Noctuidae)

Expression Profiles of the Heat Shock Protein 70 Gene in Response to Heat Stress in Agrotis c-nigrum (Lepidoptera: Noctuidae)

Cloning and expression of HSP70 gene of sipuncula Phascolosoma esculenta

Virtual screening for angiotensin I-converting enzyme inhibitory peptides from Phascolosoma esculenta

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