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:

387
مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Download:

212
مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Cites:

Information Journal Paper

Title

A NOVEL VECTOR FOR EXPRESSION/SECRETION OF PROPERLY FOLDED EUKARYOTIC PROTEINS: A COMPARATIVE STUDY ON CYTOPLASMIC AND PERIPLASMIC EXPRESSION OF HUMAN EPIDERMAL GROWTH FACTOR IN E. COLI

Pages

  51-61

Keywords

?-LACTAMASE 
HUMAN EPIDERMAL GROWTH FACTOR (HEGF) 

Abstract

 Expression of eukaryotic proteins in E. coli often results in their aggregation. Proper folding and solubility of therapeutical proteins are the pre-requisite for their bioactivity. This is not achieved in cytoplasmic expression in E. coli because of the absence of disulfide bonds formation. A novel expression/secretion vector was constructed which exploited b ?-LACTAMASE SIGNAL SEQUENCE to translocate processed and soluble proteins into the periplasm of cells. SECRETION of model proteins, b ?-LACTAMASE and human Epidermal Growth Factor (hEGF) in M15/pSB and M15/pSE systems respectively, was confirmed by SDS-PAGE analysis and bioactivity assay. Secreted hEGF was found to be identical to authentic protein, in size, N-terminal amino acid sequence, biological activity and Western-blotting. The radioimmunoassay revealed 10-fold-higher level of hEGF expression in M15/pSE SECRETION system compared to that of cytoplasmic expression of the protein. The properly processed and in vivo folded hEGF demonstrated high solubility and bioactivity. The data obtained, evidenced in favor of M15/pSE expression system, which might be suitable to produce the small eukaryotic disulfide-bonded proteins for therapeutical applications or structural studies.

Cites

  • No record.

    • References

  • No record.

    • Cite

    APA: Copy

    EBRAHIMIRAD, M., AZARNOUSH, MORTEZA, BASHIR, A., & BAKAYEV, V.V.. (2004). A NOVEL VECTOR FOR EXPRESSION/SECRETION OF PROPERLY FOLDED EUKARYOTIC PROTEINS: A COMPARATIVE STUDY ON CYTOPLASMIC AND PERIPLASMIC EXPRESSION OF HUMAN EPIDERMAL GROWTH FACTOR IN E. COLI . IRANIAN BIOMEDICAL JOURNAL, 8(2), 51-61. SID. https://sid.ir/paper/277014/en

    Vancouver: Copy

    EBRAHIMIRAD M., AZARNOUSH MORTEZA, BASHIR A., BAKAYEV V.V.. A NOVEL VECTOR FOR EXPRESSION/SECRETION OF PROPERLY FOLDED EUKARYOTIC PROTEINS: A COMPARATIVE STUDY ON CYTOPLASMIC AND PERIPLASMIC EXPRESSION OF HUMAN EPIDERMAL GROWTH FACTOR IN E. COLI . IRANIAN BIOMEDICAL JOURNAL[Internet]. 2004;8(2):51-61. Available from: https://sid.ir/paper/277014/en

    IEEE: Copy

    M. EBRAHIMIRAD, MORTEZA AZARNOUSH, A. BASHIR, and V.V. BAKAYEV, “A NOVEL VECTOR FOR EXPRESSION/SECRETION OF PROPERLY FOLDED EUKARYOTIC PROTEINS: A COMPARATIVE STUDY ON CYTOPLASMIC AND PERIPLASMIC EXPRESSION OF HUMAN EPIDERMAL GROWTH FACTOR IN E. COLI ,” IRANIAN BIOMEDICAL JOURNAL, vol. 8, no. 2, pp. 51–61, 2004, [Online]. Available: https://sid.ir/paper/277014/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