Quantification of Anti-Aggregation Activity of Chaperones: A Test-System Based on Dithiothreitol-Induced Aggregation of Bovine Serum Albumin

作者: Vera A. Borzova , Kira A. Markossian , Dmitriy A. Kara , Natalia A. Chebotareva , Valentina F. Makeeva

DOI: 10.1371/JOURNAL.PONE.0074367

关键词: ArginineUltracentrifugeChemical chaperoneGeneticsBovine serum albuminProtein quaternary structureDithiothreitolChemistryProtein aggregationPlasma protein bindingChromatographyGeneral Biochemistry, Genetics and Molecular BiologyGeneral Agricultural and Biological SciencesGeneral Medicine

摘要: The methodology for quantification of the anti-aggregation activity protein and chemical chaperones has been elaborated. applicability this was demonstrated using a test-system based on dithiothreitol-induced aggregation bovine serum albumin at 45°C as an example. Methods calculating initial rate (vagg) have discussed. comparison dependences vagg concentrations intact cross-linked α-crystallin allowed us to make conclusion that non-linear character dependence concentration due dynamic mobility quaternary structure polydispersity α-crystallin–target complexes. To characterize (arginine, arginine ethyl ester, amide proline), semi-saturation [L]0.5 used. Among studied, ester reveal highest ([L]0.5 = 53 58 mM, respectively).

参考文章(111)
Kira A. Markossian, Nikolay V. Golub, Helen A. Khanova, Dmitrii I. Levitsky, Nikolay B. Poliansky, Konstantin O. Muranov, Boris I. Kurganov, Mechanism of thermal aggregation of yeast alcohol dehydrogenase I Role of intramolecular chaperone Biochimica et Biophysica Acta. ,vol. 1784, pp. 1286- 1293 ,(2008) , 10.1016/J.BBAPAP.2008.04.030
H. August Petersen, Joseph F. Foster, THE MICROHETEROGENEITY OF PLASMA ALBUMINS. II. PREPARATION AND SOLUBILITY PROPERTIES OF SUBFRACTIONS. Journal of Biological Chemistry. ,vol. 240, pp. 2503- 2507 ,(1965) , 10.1016/S0021-9258(18)97353-9
H. August Petersen, Joseph F. Foster, The microheterogeneity of plasma albumins. 3. Comparison of some physicochemical properties of subfractions. Journal of Biological Chemistry. ,vol. 240, pp. 3858- 3865 ,(1965) , 10.1016/S0021-9258(18)97121-8
Jessica Gobbo, Caroline Gaucher-Di-Stasio, Stéphanie Weidmann, Jean Guzzo, Carmen Garrido, Quantification of HSP27 and HSP70 Molecular Chaperone Activities Methods of Molecular Biology. ,vol. 787, pp. 137- 143 ,(2011) , 10.1007/978-1-61779-295-3_11
Chaiyavat Chaiyasut, Takao Tsuda, Isoelectric Points Estimation of Proteins by Electroosmotic Flow: pH Relationship Using Physically Adsorbed Proteins on Silica Gel Chromatography : journal of separation and detection sciences = クロマトグラフィー : 分離・検出科学. ,vol. 22, pp. 91- 95 ,(2001)
Arthur Jennison Rowe, S. E. Harding, J. C. Horton, Analytical ultracentrifugation in biochemistry and polymer science Royal Society of Chemistry. ,(1992)
Boris Ivanovich Kurganov, Boris I Kurganov, VA Yakovlev, Allosteric enzymes: Kinetic behaviour ,(1982)
Tony R. Obalinsky, Protein folding : new research Nova Science. ,(2006)
Anne Marsden, Amy Shahtout, International Organization for Standardization American Society of Microbiology. pp. 447- 450 ,(2014) , 10.1128/9781555817282.CH22
Frank Ferrone, Analysis of protein aggregation kinetics. Methods in Enzymology. ,vol. 309, pp. 256- 274 ,(1999) , 10.1016/S0076-6879(99)09019-9