The Relationship between Albumin-Binding Capacity of Recombinant Polypeptide and Changes in the Structure of Albumin-Binding Domain
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| 024 | 7 | 0 | |a 10.1007/s10517-015-2972-z |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s10517-015-2972-z | ||
| 245 | 0 | 4 | |a The Relationship between Albumin-Binding Capacity of Recombinant Polypeptide and Changes in the Structure of Albumin-Binding Domain |h [Elektronische Daten] |c [E. Bormotova, T. Gupalova] |
| 520 | 3 | |a Many bacteria express surface proteins interacting with human serum albumin (HSA). One of these proteins, PAB from anaerobic bacteria, contains an albumin-binding domain consisting of 45 amino acid residues known as GA domain. GA domains are also found in G proteins isolated from human streptococcal strains (groups C and G) and of albumin-binding protein isolated from group G streptococcal strains of animal origin. The GA domain is a left-handed three-helix bundle structure in which amino acid residues of the second and third helixes are involved in albumin binding. We studied the relationship between HSA-binding activity of the recombinant polypeptide isolated from group G streptococcus of animal origin and structure of the GA domain is studied. Structural changes in GA domain significantly attenuated HAS-binding capacity of the recombinant polypeptide. Hence, affinity HSA-binding polypeptide depends on stability of GA domain structure. | |
| 540 | |a Springer Science+Business Media New York, 2015 | ||
| 690 | 7 | |a recombinant polypeptide |2 nationallicence | |
| 690 | 7 | |a GA domain |2 nationallicence | |
| 690 | 7 | |a three-helix bundle structure |2 nationallicence | |
| 700 | 1 | |a Bormotova |D E. |u Department of Molecular Microbiology, Institute of Experimental Medicine, St. Petersburg, Russia |4 aut | |
| 700 | 1 | |a Gupalova |D T. |u Department of Molecular Microbiology, Institute of Experimental Medicine, St. Petersburg, Russia |4 aut | |
| 773 | 0 | |t Bulletin of Experimental Biology and Medicine |d Springer US; http://www.springer-ny.com |g 159/3(2015-07-01), 393-397 |x 0007-4888 |q 159:3<393 |1 2015 |2 159 |o 10517 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s10517-015-2972-z |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a research-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s10517-015-2972-z |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Bormotova |D E. |u Department of Molecular Microbiology, Institute of Experimental Medicine, St. Petersburg, Russia |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Gupalova |D T. |u Department of Molecular Microbiology, Institute of Experimental Medicine, St. Petersburg, Russia |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Bulletin of Experimental Biology and Medicine |d Springer US; http://www.springer-ny.com |g 159/3(2015-07-01), 393-397 |x 0007-4888 |q 159:3<393 |1 2015 |2 159 |o 10517 | ||