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Pregled bibliografske jedinice broj: 1266892

Glycoproteomics meets thermodynamics: A calorimetric study of the effect of sialylation and synergistic anion on the binding of iron to human serum transferrin


Borko, Valentina Borko; Friganović, Tomislav; Weitner, Tin
Glycoproteomics meets thermodynamics: A calorimetric study of the effect of sialylation and synergistic anion on the binding of iron to human serum transferrin // Journal of inorganic biochemistry, 244 (2023), 112207, 12 doi:10.1016/j.jinorgbio.2023.112207 (međunarodna recenzija, članak, znanstveni)


CROSBI ID: 1266892 Za ispravke kontaktirajte CROSBI podršku putem web obrasca

Naslov
Glycoproteomics meets thermodynamics: A calorimetric study of the effect of sialylation and synergistic anion on the binding of iron to human serum transferrin

Autori
Borko, Valentina Borko ; Friganović, Tomislav ; Weitner, Tin

Izvornik
Journal of inorganic biochemistry (0162-0134) 244 (2023); 112207, 12

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
Human serum transferrin ; Sialic acid ; Synergistic anion ; Glycoproteomics ; Isothermal titration calorimetry ; Thermodynamics

Sažetak
The thermodynamic parameters for the binding of ferric ions to human serum transferrin (hTf) as the major mediator of iron transport in blood plasma were determined by isothermal titration calorimetry in the presence of carbonate and oxalate as synergistic anions at pH 7.4. The results indicate that the binding of ferric ions to the two binding sites of hTf is driven both enthalpically and entropically in a lobe-dependent manner: binding to the C-site is mainly enthalpically driven, whereas binding to the N- site is mainly entropically driven. Lower sialic acid content of hTf leads to more exothermic apparent binding enthalpies for both lobes, while the increased apparent binding constants for both sites were found in the presence of carbonate. Sialylation also unequally affected the heat change rates for both sites only in the presence of carbonate, but not in the presence of oxalate. Overall, the results suggest that the desialylated hTf has a higher iron sequestering ability, which may have implications for iron metabolism.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Farmacija



POVEZANOST RADA


Projekti:
UIP-2017-05-9537 - Glikozilacija serumskog transferina kao faktor u mehanizmu prijenosa željeza (GlyMech) (Weitner, Tin, HRZZ - 2017-05) ( CroRIS)
EK-EFRR-KK.01.1.1.02.0021 - Jačanje znanstveno-istraživačkih i inovacijskih kapaciteta Farmaceutsko-biokemijskog fakulteta Sveučilišta u Zagrebu (FarmInova) (Lovrić, Jasmina, EK - Ulaganje u organizacijsku reformu i infrastrukturu u sektoru istraživanja, razvoja i inovacija) ( CroRIS)
EK-KF-KK.01.1.1.01.0010 - Znanstveni centar izvrsnosti za personaliziranu brigu o zdravlju (ZCIPersonHealth) (Polašek, Ozren; Secenji, Aleksandar, EK ) ( CroRIS)
--KK.01.1.1.07.0055 - Razvoj metoda za proizvodnju i obilježavanje glikanskih standarda za molekularnu dijagnostiku (Gabričević, Mario) ( CroRIS)

Ustanove:
Farmaceutsko-biokemijski fakultet, Zagreb

Profili:

Avatar Url Tin Weitner (autor)

Avatar Url Tomislav Friganović (autor)

Avatar Url Valentina Borko (autor)

Poveznice na cjeloviti tekst rada:

doi www.sciencedirect.com

Citiraj ovu publikaciju:

Borko, Valentina Borko; Friganović, Tomislav; Weitner, Tin
Glycoproteomics meets thermodynamics: A calorimetric study of the effect of sialylation and synergistic anion on the binding of iron to human serum transferrin // Journal of inorganic biochemistry, 244 (2023), 112207, 12 doi:10.1016/j.jinorgbio.2023.112207 (međunarodna recenzija, članak, znanstveni)
Borko, V., Friganović, T. & Weitner, T. (2023) Glycoproteomics meets thermodynamics: A calorimetric study of the effect of sialylation and synergistic anion on the binding of iron to human serum transferrin. Journal of inorganic biochemistry, 244, 112207, 12 doi:10.1016/j.jinorgbio.2023.112207.
@article{article, author = {Borko, Valentina Borko and Friganovi\'{c}, Tomislav and Weitner, Tin}, year = {2023}, pages = {12}, DOI = {10.1016/j.jinorgbio.2023.112207}, chapter = {112207}, keywords = {Human serum transferrin, Sialic acid, Synergistic anion, Glycoproteomics, Isothermal titration calorimetry, Thermodynamics}, journal = {Journal of inorganic biochemistry}, doi = {10.1016/j.jinorgbio.2023.112207}, volume = {244}, issn = {0162-0134}, title = {Glycoproteomics meets thermodynamics: A calorimetric study of the effect of sialylation and synergistic anion on the binding of iron to human serum transferrin}, keyword = {Human serum transferrin, Sialic acid, Synergistic anion, Glycoproteomics, Isothermal titration calorimetry, Thermodynamics}, chapternumber = {112207} }
@article{article, author = {Borko, Valentina Borko and Friganovi\'{c}, Tomislav and Weitner, Tin}, year = {2023}, pages = {12}, DOI = {10.1016/j.jinorgbio.2023.112207}, chapter = {112207}, keywords = {Human serum transferrin, Sialic acid, Synergistic anion, Glycoproteomics, Isothermal titration calorimetry, Thermodynamics}, journal = {Journal of inorganic biochemistry}, doi = {10.1016/j.jinorgbio.2023.112207}, volume = {244}, issn = {0162-0134}, title = {Glycoproteomics meets thermodynamics: A calorimetric study of the effect of sialylation and synergistic anion on the binding of iron to human serum transferrin}, keyword = {Human serum transferrin, Sialic acid, Synergistic anion, Glycoproteomics, Isothermal titration calorimetry, Thermodynamics}, chapternumber = {112207} }

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


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