Intermolecular interactions in solutions of serum albumin
The mechanisms of intermolecular protein complex formation were studied by the example of monomers, oligomers and aggregates of bovine serum albumin (BSA) depending on the protein concentration, pH and urea concentration. Using dynamic light scattering (DLS), analytical ultracentrifugation (AUC) and...
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| Veröffentlicht in: | Cell and tissue biology 2017, Vol.11 (1), p.9-15 |
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| creator | Polyanichko, A. M. Mikhailov, N. V. Romanov, N. M. Baranova, Yu. G. Chikhirzhina, E. V. |
| description | The mechanisms of intermolecular protein complex formation were studied by the example of monomers, oligomers and aggregates of bovine serum albumin (BSA) depending on the protein concentration, pH and urea concentration. Using dynamic light scattering (DLS), analytical ultracentrifugation (AUC) and PAG electrophoresis we have shown the existence of dynamic equilibrium between monomers and aggregates in BSA solution. Decreasing pH of the solution (4.0–1.0) resulted in increasing sizes of the aggregates. In the solutions with low urea concentrations (below 2 M) the sizes of aggregates decreased, while higher urea concentrations (2–8 M) induced formation of larger aggregates due to the unfolding of the protein. |
| doi_str_mv | 10.1134/S1990519X17010084 |
| format | Article |
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In the solutions with low urea concentrations (below 2 M) the sizes of aggregates decreased, while higher urea concentrations (2–8 M) induced formation of larger aggregates due to the unfolding of the protein.</description><identifier>ISSN: 1990-519X</identifier><identifier>EISSN: 1990-5203</identifier><identifier>DOI: 10.1134/S1990519X17010084</identifier><language>eng</language><publisher>Moscow: Pleiades Publishing</publisher><subject>Biomedical and Life Sciences ; Bovine serum albumin ; Cell Biology ; Life Sciences ; Light scattering ; Monomers ; pH effects ; Protein folding ; Proteins ; Ultracentrifugation ; Urea</subject><ispartof>Cell and tissue biology, 2017, Vol.11 (1), p.9-15</ispartof><rights>Pleiades Publishing, Ltd. 2017</rights><rights>Copyright Springer Science & Business Media 2017</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c2314-2ce0d6d629e34b31706c3618865d47db19ed2f5f4a714419a9619ba2c2bd3073</citedby><cites>FETCH-LOGICAL-c2314-2ce0d6d629e34b31706c3618865d47db19ed2f5f4a714419a9619ba2c2bd3073</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1134/S1990519X17010084$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1134/S1990519X17010084$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids></links><search><creatorcontrib>Polyanichko, A. 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| language | eng |
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| source | SpringerNature Journals |
| subjects | Biomedical and Life Sciences Bovine serum albumin Cell Biology Life Sciences Light scattering Monomers pH effects Protein folding Proteins Ultracentrifugation Urea |
| title | Intermolecular interactions in solutions of serum albumin |
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