PURIFICATION AND CHARACTERIZATION OF HISTIDINE-TAGGED RECOMBINANT HBEAG

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ARASHKIYA A.; ROUHVAND F.; SADAT S.M.; AMINI SAFIEH; ANDALIBI S.; FOROUZANDEH M.

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Journal: Physiology and Pharmacology Year:2005 | Volume:8 | Issue:2 Page(s): 125-136

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Title

PURIFICATION AND CHARACTERIZATION OF HISTIDINE-TAGGED RECOMBINANT HBEAG

Author(s)

Keywords

RECOMBINANT HBEAGQ4

HISTIDINE TAGQ4

PHYSIOLOGICAL CHARACTERISTICSQ4

NI-NTA COLUMN CHROMATOGRAPHYQ4

PQE30Q4

Abstract

Hepatitis B virus (HBV) is considered a global health problem whid. affects 360 millions of people worldwide and about two millions in Iran. Among HBV antigens, the physiological function of HBeAg is still unresolved. In this respect, its presence in positive patients is regarded as a marker of viral replication and it may have roles in pathogenesis and persistence of the disease, while no obvious changes in clinical course of the disease has been observed in negative patients. As a result, availability of this protein with characteristics of the naturally occurred antigen in high amounts and of the same purity is highly required for being. Utilized in medical research and diagnosis. At present, RECOMBINANT HBEAG is being produced in different expression systems for various applications. In the present study, by application of a simple expression/purification system in E. coli and with the aim of producing physiologically natural HBeAg, that portion of the gene, which exactly corresponds to amino acid sequence of the blood-borne HBeAg have been isolated and cloned into pQE-30 vector which adds a 6x Histag to the N-terminal of the inserted gene, providing the ability of one step purification method by exploiting NI-NTA COLUMN CHROMATOGRAPHY. Following restriction analysis and confirmation of recombinant vector accuracy, transformation to E. coli M15 cells and IPTG-mediated induction for protein expression was performed. Analysis of the purified protein by SOS-PAGE, ELISA and Western blotting indicated that obtained RECOMBINANT HBEAG had the perfect antigenic properties of authentic HBeAg and addition of the His-tag segment which produces extra epitopes on this antigen had no adverse effect on these properties. The results of this study clearly describe a very simple and efficient system for providing RECOMBINANT HBEAG in high yield and purity for diagnostic and physiological research applications.

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References

SEROEPIDEMIOLOGY OF HEPATITIS B AND C IN BLOOD DONORS IN KASHAN, 1996-2001

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APA: Copy

ARASHKIYA, A., ROUHVAND, F., SADAT, S.M., AMINI, SAFIEH, ANDALIBI, S., & FOROUZANDEH, M.. (2005). PURIFICATION AND CHARACTERIZATION OF HISTIDINE-TAGGED RECOMBINANT HBEAG. PHYSIOLOGY AND PHARMACOLOGY, 8(2), 125-136. SID. https://sid.ir/paper/75110/en

Vancouver: Copy

ARASHKIYA A., ROUHVAND F., SADAT S.M., AMINI SAFIEH, ANDALIBI S., FOROUZANDEH M.. PURIFICATION AND CHARACTERIZATION OF HISTIDINE-TAGGED RECOMBINANT HBEAG. PHYSIOLOGY AND PHARMACOLOGY[Internet]. 2005;8(2):125-136. Available from: https://sid.ir/paper/75110/en

IEEE: Copy

A. ARASHKIYA, F. ROUHVAND, S.M. SADAT, SAFIEH AMINI, S. ANDALIBI, and M. FOROUZANDEH, “PURIFICATION AND CHARACTERIZATION OF HISTIDINE-TAGGED RECOMBINANT HBEAG,” PHYSIOLOGY AND PHARMACOLOGY, vol. 8, no. 2, pp. 125–136, 2005, [Online]. Available: https://sid.ir/paper/75110/en

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