The binding of Ca2+ and Mg2+ to human serium albumin: A calorimetric study

Analysis of the mechanism of the magnesium effect on the warfarin-albumin interaction

“…A difference in the affinity of albumin in the two distinct conformational states for Mg2+ is in accordance with a calorimetric study [4] showing that the binding of Mg2' to albumin increases with pH, unfortunately it is not possible to calculate a binding constant at different pH's from this study. It cannot be excluded, however, that in the N conformation the binding sites for Mg2+ and warfarin are farther apart than in the B conformation and therefore, that the binding of Mg*+ does not interfere with the binding of warfarin when the protein is in the N conformation.…”

“…Pedersen [3] and Eatough et al [4] found evidence that Ca'-and Mg" share their binding sites on the albumin molecule. Therefore the effect of Mg2+ on the binding of warfarin to albumin can be expected to be similar to the effect of Ca'-.…”

“…regardless of whether the protein is in the N or in the B conformation. The difference between the effects of Mg" and Ca?+ on the warfarin-albumin interaction is surprising because Mgz+ and Ca?+ should share their binding sites on the albumin molecule [3,4].…”

Ischemia-modified albumin: Crosstalk between fatty acid and cobalt binding

“…Albumin is an important transporter of Ca 2+ in blood plasma. Many reports suggest that this occurs in a non-specific fashion, involving various carboxylate side chains on the surface of albumin [42] , [62] , while work by Majorek et al. detected three defined Ca 2+ binding sites on bovine albumin [63] .…”

Thermodynamics of the Interactions of Aminobisphosphonates and Their Calcium Complexes with Bovine Serum Albumin

“…Albumin is a main circulatory protein involved in the handling of Ca 2+ in all mammals that controls the level of this cation (as well as Mg 2+ ) in the blood. Binding of Ca 2+ to serum albumin is characterized by low affinity ( K = 1.5 × 10 3 , 5.24 × 10 2 ) and high capacity; approximately 45% of 2.4 m m Ca 2+ floating in the serum is albumin‐bound or ‐ as other authors describe; albumin‐associated . A bovine serum albumin (BSA) presents 76% sequence identity with the HSA and is often used as a model protein for various interaction studies, and we decided to use it as well in presented article.…”