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Mazloomrezaei, Mohsen, Hosseini, Mahsa, Ahmadi, Nahid, Mahmoudi Maymand, Elham, Eftekhar, Ebrahim, Asgari, Amir, Ramezani, Amin. (1401). Introducing a New Method for Purification of Human IL-4 by Substitution of a Single Amino Acid in IL-4 Protein Sequence. سامانه مدیریت نشریات علمی, 19(4), 436-445. doi: 10.22034/iji.2022.94985.2336
Mohsen Mazloomrezaei; Mahsa Sadat Hosseini; Nahid Ahmadi; Elham Mahmoudi Maymand; Ebrahim Eftekhar; Amir Asgari; Amin Ramezani. "Introducing a New Method for Purification of Human IL-4 by Substitution of a Single Amino Acid in IL-4 Protein Sequence". سامانه مدیریت نشریات علمی, 19, 4, 1401, 436-445. doi: 10.22034/iji.2022.94985.2336
Mazloomrezaei, Mohsen, Hosseini, Mahsa, Ahmadi, Nahid, Mahmoudi Maymand, Elham, Eftekhar, Ebrahim, Asgari, Amir, Ramezani, Amin. (1401). 'Introducing a New Method for Purification of Human IL-4 by Substitution of a Single Amino Acid in IL-4 Protein Sequence', سامانه مدیریت نشریات علمی, 19(4), pp. 436-445. doi: 10.22034/iji.2022.94985.2336
Mazloomrezaei, Mohsen, Hosseini, Mahsa, Ahmadi, Nahid, Mahmoudi Maymand, Elham, Eftekhar, Ebrahim, Asgari, Amir, Ramezani, Amin. Introducing a New Method for Purification of Human IL-4 by Substitution of a Single Amino Acid in IL-4 Protein Sequence. سامانه مدیریت نشریات علمی, 1401; 19(4): 436-445. doi: 10.22034/iji.2022.94985.2336

Introducing a New Method for Purification of Human IL-4 by Substitution of a Single Amino Acid in IL-4 Protein Sequence

Iranian Journal of Immunology
دوره 19، شماره 4، اسفند 2022، صفحه 436-445    اصل مقاله (2.46 M)
نوع مقاله: Original Article
شناسه دیجیتال (DOI): 10.22034/iji.2022.94985.2336
نویسندگان
Mohsen Mazloomrezaei1؛ Mahsa Sadat Hosseini1؛ Nahid Ahmadi1، 2؛ Elham Mahmoudi Maymand1؛ Ebrahim Eftekhar3؛ Amir Asgari4؛ Amin Ramezani* 1، 2
1Shiraz Institute for Cancer Research, School of Medicine, Shiraz University of Medical Sciences, Shiraz, Iran
2Department of Medical Biotechnology, School of Advanced Medical Sciences and Technologies, Shiraz University of Medical Sciences, Shiraz, Iran
3Molecular Medicine Research Center, Hormozgan Health Institute, Hormozgan University of Medical Sciences, Bandar Abbas, Iran
4Faculty of Pharmacy and Pharmaceutical Sciences, University of Alberta, Edmonton, Alberta, Canada
چکیده
Background: It is advantageous to develop an effective purification procedure to produce recombinant protein drugs (rPDs) without any tags. To remove N- or C-terminus tags from the rPDs, several cleavage site-based endopeptidases were used. Separating the endopeptidase enzyme from the rPDs is a time-consuming and costly process.
Objective: To design and develop a new method for the purification of human interleukin (IL)-4 with potential application for other cytokines.
Methods: Met-like amino acids were substituted at position 120 to reduce the possibility of alteration in the structure of IL-4 and its biological activity. Based on the in silico analysis, isoleucine was chosen as an alternative amino acid, and the M120I mutant IL-4 (mIL-4) model was selected for the downstream analysis. Recombinant mIL-4 was produced in the E.coli BL21 host and purified with CNBr. Then in vitro evaluations of the native and mutant IL-4 were performed.
Results: The results showed that both the native and mutant IL-4 had the same effect on TF-1 cell proliferation. On the other hand, there was no significant difference between the effects of native IL-4 (nIL-4) and mIL-4 on the expression of IL-4 and IL-10 in activated peripheral blood mononuclear cells. Native and mutant IL-4 have similar biological activities.
Conclusion: Here, an efficient and straightforward system is introduced to purify IL-4 cytokine using CNBr, which could be applied to other rPDs.
کلیدواژه‌ها
Cyanogen Bromide؛ Interleukin-4؛ Protein Purification؛ Tag removal
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