Perbedaan Profil Protein Plasma Darah Mencit Menggunakan SDS-PAGE Tanpa Penambahan dan dengan Penambahan 2-Mercaptoethanol
DOI:
https://doi.org/10.23887/jjpb.v11i2.82139Keywords:
mice, protein profile, blood plasma, SDS-PAGE, 2-mercaptoethanolAbstract
SDS-PAGE is a method used to analyze proteins based on differences in molecular weight. Sample preparation in SDS-PAGE with 2-mercaptoethanol will reduce disulfide bonds in proteins. The sulfide bond reduction process will cause differences in protein conformation and profile. The purpose of this study was to compare the pattern of blood plasma protein profiles of mice analyzed using SDS-PAGE, with the addition of 2-mercaptoethanol and without the addition of 2-mercaptoethanol in a mixture of sample buffer solutions. The results of SDS-PAGE showed that the blood plasma protein profile of mice without the addition and with the addition of 2-mercaptoethanol showed differences in the number of protein bands, the molecular weight of several proteins and the thickness of the protein bands. There were nine protein bands with a molecular weight above 52 kDa in the profile without the addition of 2-mercaptoethanol, while there were only five protein bands with a molecular weight above 52 kDa in the profile with the addition of 2-mercaptoethanol. The difference in protein profile patterns shows that mouse blood plasma contains proteins containing disulfide bonds that can be reduced by 2-mercaptoethanol.
References
Butera, D., Cook, K. M., Chiu, J., Wong, J. W. H., & Hogg, P. J. (2014). Control of blood proteins by functional disulfide bonds. Blood, 123(13), 2000–2007. https://doi.org/10.1182/blood-2014-01-549816
Carson, S., Miller, H. B., Witherow, D. S., & Srougi, M. C. (2019). Molecular Biology Techniques A Classroom Laboratory Manual Fourth Edition. Academic Press.
Carvalho, F. A. O., Carvalho, J. W. P., Santiago, P. S., & Tabak, M. (2011). Further characterization of the subunits of the giant extracellular hemoglobin of Glossoscolex paulistus (HbGp) by SDS-PAGE electrophoresis and MALDI-TOF-MS. Process Biochemistry, 46(11), 2144–2151. https://doi.org/10.1016/j.procbio.2011.08.013
Clark, D. P., Pazdernik, N. J., & McGehee, M. . (2019). Molecular Biology. Academic Cell.
Çolak, R., Yigit, N., Çolak, E., Gattermann, R., & Neumann, K. (2002). SDS-PAGE Patterns
of Blood Serum Proteins in some Species of the Genus Meriones (Mammalia: Rodentia). In Turk Journal Zoology (Vol. 26, pp. 177–181). http://journals.tubitak.gov.tr/zoology/issues/zoo-02-26-2/zoo-26-2-5-0110-2.pdf
Hermanson, G. . (2013). Bioconjugate Techniques. Academic Press.
Hidayati, D., Abdulgani, N., Setiyawan, H., Trisnawati, I., Ashuri, N. M., & Sa’adah, N. N.
(2017). Analysis of protein profiles in diabetic rat blood plasma that induced by alloxan. Proceeding of International Biology Conference AIP, 020016. https://doi.org/10.1063/1.4985407
Kleinman, W. A., & Richie, J. P. (2000). Status of glutathione and other thiols and disulfides
in human plasma. Biochemical Pharmacology, 60(1), 19–29. https://doi.org/10.1016/S0006-2952(00)00293-8
Kreyling, W. G., Fertsch-Gapp, S., Schäffler, M., Johnston, B. D., Haberl, N., Pfeiffer, C.,
Diendorf, J., Schleh, C., Hirn, S., Semmler-Behnke, M., Epple, M., & Parak, W. J. (2014). In vitro and in vivo interactions of selected nanoparticles with rodent serum proteins and their consequences in biokinetics. Beilstein Journal of Nanotechnology, 5, 1699–1711. https://doi.org/10.3762/bjnano.5.180
Mthembu, S. N., Sharma, A., Albericio, F., & de la Torre, B. G. (2020). Breaking a Couple:
Disulfide Reducing Agents. ChemBioChem, 21(14), 1947–1954. https://doi.org/10.1002/cbic.202000092
O’Connor, C. M. (2022). INVESTIGATIONS IN MOLECULAR CELL BIOLOGY. Boston
College.
Qi, P. X., & Onwulata, C. I. (2011). Physical properties, molecular structures, and protein
quality of texturized whey protein isolate: Effect of extrusion moisture content. Journal of Dairy Science, 94(5), 2231–2244. https://doi.org/10.3168/jds.2010-3942
Shibata, H., Kato, H., & Oda, J. (1998). Random mutagenesis on the Pseudomonas lipase
activator protein, LipB: exploring amino acid residues required for its function. Protein Engineering Design and Selection, 11(6), 467–472. https://doi.org/10.1093/protein/11.6.467
Susanti, A. M., Darmawati, S., & Maharani, E. T. W. (2019). Profil Protein Lima Jenis Daging
yang Direndam Daun Pepaya Berbasis SDS-PAGE. Gorontalo Journal of Public Health, 2(1), 132. https://doi.org/10.32662/gjph.v2i1.482
Xu, X., Chiu, J., Chen, S., & Fang, C. (2021). Pathophysiological roles of cell surface and
extracellular protein disulfide isomerase and their molecular mechanisms. British Journal of Pharmacology, 178(15), 2911–2930. https://doi.org/10.1111/bph.15493
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