Microcalorimetric studies on the interactions of lanthanide ions with bovine serum albumin

Li, X.; Wang, C.; Li, J.; Wang, Z.

doi:10.1007/s10973-006-7611-5

Cited by 6 publications

(2 citation statements)

References 17 publications

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“…These results are in agreement with the general concept that postulates the coexistence of binding sites with different affinities for the ligand within a single protein molecule. The n values determined from Eu 3+ luminescence measurements in this work are in good agreement with the literature data; e.g., the results of Li et al 42 are close to the parameters obtained from the Scatchard plots presented in Figure 4. In contrast, the number of binding sites n obtained from fluorescence quenching curves is equal to unity (Table 1).…”

Section: ■ Discussionsupporting

confidence: 91%

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Assessment of the Europium(III) Binding Sites on Albumin Using Fluorescence Spectroscopy

et al. 2014

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Intrinsic fluorescence quenching of bovine serum albumin (BSA) and europium(III) luminescence in BSA complexes were investigated. The number of BSA binding sites (n) and equilibrium constant (Keq) values were determined from both measurements provided qualitatively different results. While the modified Stern-Volmer relation for BSA fluorescence quenching gave n = 1 at pH 4.5 and pH 6, two sets of binding sites were determined from Eu(3+) luminescence with n1 = 2, n2 = 4 at pH 6 and n1 = 1, n2 = 2 at pH 4.5. The model explaining the discrepancy between the results obtained by these fluorescent approaches was suggested, and the limitations in application of the "log-log" Stern-Volmer plots in analysis of binding processes were discussed.

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Section: ■ Discussionsupporting

confidence: 91%

“…41 Finally, interaction of BSA and Eu 3+ was studied by microcalorimetry. 42 Authors suggested the existence of two classes of binding sites with n 1 = 1.7 for highaffinity specific sites and n 2 = 6.6 for nonspecific ones.…”

Section: ■ Discussionmentioning

confidence: 99%

Assessment of the Europium(III) Binding Sites on Albumin Using Fluorescence Spectroscopy

et al. 2014

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Site‐Specific Labeling of Proteins with a Chemically Stable, High‐Affinity Tag for Protein Study

Yang

Cao

et al. 2012

Chemistry A European J

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Site-specific labeling of proteins with paramagnetic lanthanides offers unique opportunities by virtue of NMR spectroscopy in structural biology. In particular, these paramagnetic data, generated by the anisotropic paramagnetism including pseudocontact shifts (PCS), residual dipolar couplings (RDC), and paramagnetic relaxation enhancement (PRE), are highly valuable in structure determination and mobility studies of proteins and protein-ligand complexes. Herein, we present a new way to label proteins in a site-specific manner with a high-affinity and chemically stable tag, 4-vinyl(pyridine-2,6-diyl)bismethylenenitrilo tetrakis(acetic acid) (4VPyMTA), through thiol alkylation. Its performance has been demonstrated in G47C and E64C mutants of human ubiquitin both in vitro and in a crowded environment. In comparison with the published tags, 4VPyMTA has several interesting features: 1) it has a very high binding affinity for lanthanides (higher than EDTA), 2) there is no heterogeneity in complexes with lanthanides, 3) the derivatized protein is stable and potentially applicable to the in situ analysis of proteins.

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Effect of berberine alkaloids on Bifidobacterium adolescentis growth by microcalorimetry

Yan¹,

Han

Wei³

et al. 2009

J Therm Anal Calorim

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Microcalorimetric studies on the interactions of lanthanide ions with bovine serum albumin

Cited by 6 publications

References 17 publications

Assessment of the Europium(III) Binding Sites on Albumin Using Fluorescence Spectroscopy

Assessment of the Europium(III) Binding Sites on Albumin Using Fluorescence Spectroscopy

Site‐Specific Labeling of Proteins with a Chemically Stable, High‐Affinity Tag for Protein Study

Effect of berberine alkaloids on Bifidobacterium adolescentis growth by microcalorimetry

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