مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

video

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

sound

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Persian Version

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

View:

30
مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Download:

15
مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Cites:

Information Journal Paper

Title

Recombinant Protein Purification using Composite Polyacrylamide-Nanocrystalline Cryogel Monolith Column and Carbohydrate-Binding Module Family 64 as Affinity Tag

Pages

  252-261

Abstract

 Background: In the field of recombinant protein production, downstream processing, especially protein purification, is critical and often the most expensive step. Carbohydrate binding module 64 (CBM64) was shown in 2011 to bind efficiently to a broad range of cellulose materials. Methods: In this study, we developed a protein purification method using nanocrystalline cellulose embedded in a polyacrylamide monolith cryogel and CBM64 affinity tag linked by intein to PD1 as a model protein. The CBM64-Intein-PD1 gene cassette was expressed in E. coli. Following cell lysis, CBM64-Intein-PD1 protein bound to the monolith PA-NCC cryogel. After washing and reducing the pH from 8. 0 to 6. 5, the intein underwent self-cleavage, resulting in the release and elution of pure PD1 protein. Results: The synthesized monolith column had a porous structure with an average pore size of 30 μ, m and a maximum binding capacity of 497 μ, g per gram of dried column. The yield of this purification method was 84%, while the yield of the His tag-acquired CBM64-Intein-PD1 method was 89%. Conclusions: We used cellulose as support for affinity chromatography, which can be used as a costeffective method for protein purification.

Multimedia

  • No record.
  • Cites

  • No record.
  • References

  • No record.
  • Cite

    APA: Copy

    Danaeifar, Mohsen, VEISI MALEKSHAHI, ZIBA, KAZEMI LOMEDASHT, FATEMEH, & Mazlomi, Mohammad Ali. (2022). Recombinant Protein Purification using Composite Polyacrylamide-Nanocrystalline Cryogel Monolith Column and Carbohydrate-Binding Module Family 64 as Affinity Tag. REPORTS OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, 11(2), 252-261. SID. https://sid.ir/paper/1131504/en

    Vancouver: Copy

    Danaeifar Mohsen, VEISI MALEKSHAHI ZIBA, KAZEMI LOMEDASHT FATEMEH, Mazlomi Mohammad Ali. Recombinant Protein Purification using Composite Polyacrylamide-Nanocrystalline Cryogel Monolith Column and Carbohydrate-Binding Module Family 64 as Affinity Tag. REPORTS OF BIOCHEMISTRY AND MOLECULAR BIOLOGY[Internet]. 2022;11(2):252-261. Available from: https://sid.ir/paper/1131504/en

    IEEE: Copy

    Mohsen Danaeifar, ZIBA VEISI MALEKSHAHI, FATEMEH KAZEMI LOMEDASHT, and Mohammad Ali Mazlomi, “Recombinant Protein Purification using Composite Polyacrylamide-Nanocrystalline Cryogel Monolith Column and Carbohydrate-Binding Module Family 64 as Affinity Tag,” REPORTS OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, vol. 11, no. 2, pp. 252–261, 2022, [Online]. Available: https://sid.ir/paper/1131504/en

    Related Journal Papers

  • No record.
  • Related Seminar Papers

  • No record.
  • Related Plans

  • No record.
  • Recommended Workshops






    Move to top
    telegram sharing button
    whatsapp sharing button
    linkedin sharing button
    twitter sharing button
    email sharing button
    email sharing button
    email sharing button
    sharethis sharing button