izpis_h1_title_alt

Phase stability of aqueous mixtures of bovine serum albumin with low molecular mass salts in presence of polyethylene glycol
ID Džudžević Čančar, Hurija (Avtor), ID Belak Vivod, Matic (Avtor), ID Vlachy, Vojko (Avtor), ID Lukšič, Miha (Avtor)

.pdfPDF - Predstavitvena datoteka, prenos (505,22 KB)
MD5: CDD9DAF3C6870ED22CA7677CDA05688F
URLURL - Izvorni URL, za dostop obiščite https://www.sciencedirect.com/science/article/pii/S0167732222000125 Povezava se odpre v novem oknu

Izvleček
The stability of bovine serum albumin (BSA) solutions against phase separation caused by cooling the system is studied under the combined influence of added poly(ethylene glycol) (PEG) and alkali halide salts in water as solvent. The phase stability of the system depends on the concentration of the added PEG and its molecular mass, the concentration of the low molecular mass electrolyte and its nature, as also on the pH of the solution. More specifically, the addition of NaCl to the BSA-PEG mixture promotes phase separation at pH = 4.0, where BSA carries the net positive charge in aqueous solution, and it increases the stability of the solution at pH = 4.6, i.e., near the isoionic point of the protein. Moreover, at pH = 4.6, the cloud-point temperature decreases in the order from NaF to NaI and from LiCl to CsCl. The order of the salts at pH = 4.0 is exactly reversed: LiCl and NaF show the weakest effect on the cloud-point temperature and the strongest decrease in stability is caused by RbCl and NaNO$_3$. An attempt is made to correlate these observations with the free energies of hydration of the added salt ions and with the effect of adsorption of salt ions on the protein surface on the protein–protein interactions. Kosmotropic salt ions decrease the phase stability of BSA-PEG-salt solutions at pH < pI, while exactly the opposite is true at pH = pI.

Jezik:Angleški jezik
Ključne besede:bovine serum albumin solution, polyethylene glycol, cloud–point temperature, solubility, salt specific effects
Vrsta gradiva:Članek v reviji
Tipologija:1.01 - Izvirni znanstveni članek
Organizacija:FKKT - Fakulteta za kemijo in kemijsko tehnologijo
Status publikacije:Objavljeno
Različica publikacije:Objavljena publikacija
Leto izida:2022
Št. strani:8 str.
Številčenje:Vol. 349, art. 118477
PID:20.500.12556/RUL-137624 Povezava se odpre v novem oknu
UDK:577.322
ISSN pri članku:0167-7322
DOI:10.1016/j.molliq.2022.118477 Povezava se odpre v novem oknu
COBISS.SI-ID:93209859 Povezava se odpre v novem oknu
Datum objave v RUL:23.06.2022
Število ogledov:773
Število prenosov:133
Metapodatki:XML RDF-CHPDL DC-XML DC-RDF
:
Kopiraj citat
Objavi na:Bookmark and Share

Gradivo je del revije

Naslov:Journal of molecular liquids
Skrajšan naslov:J. mol. liq.
Založnik:Elsevier
ISSN:0167-7322
COBISS.SI-ID:15382277 Povezava se odpre v novem oknu

Licence

Licenca:CC BY-NC-ND 4.0, Creative Commons Priznanje avtorstva-Nekomercialno-Brez predelav 4.0 Mednarodna
Povezava:http://creativecommons.org/licenses/by-nc-nd/4.0/deed.sl
Opis:Najbolj omejujoča licenca Creative Commons. Uporabniki lahko prenesejo in delijo delo v nekomercialne namene in ga ne smejo uporabiti za nobene druge namene.

Sekundarni jezik

Jezik:Slovenski jezik
Ključne besede:goveji serumski albumin, vodne raztopine, fazna stabilnost, polietilen glikol, topnost

Projekti

Financer:ARRS - Agencija za raziskovalno dejavnost Republike Slovenije
Številka projekta:P1-0201
Naslov:Fizikalna kemija

Financer:ARRS - Agencija za raziskovalno dejavnost Republike Slovenije
Številka projekta:J1-1708
Naslov:Raziskave agregacije proteinov v vodnih raztopinah soli in drugih topnih dodatkov

Financer:ARRS - Agencija za raziskovalno dejavnost Republike Slovenije
Številka projekta:J1-2471
Naslov:Kemijska karcinogeneza: mehanistični vpogled

Financer:NIH - National Institutes of Health
Program financ.:RM1
Številka projekta:RM1-GM135136
Naslov:Solvation modeling for next-gen biomolecule simulations

Podobna dela

Podobna dela v RUL:
Podobna dela v drugih slovenskih zbirkah:

Nazaj