2014
DOI: 10.1016/j.chemosphere.2014.05.018
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Binding between lead ions and the high-abundance serum proteins

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Cited by 11 publications
(9 citation statements)
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“…Albumin is the most abundant plasma protein, which serves to buffer the blood, maintain the osmotic pressure, and as a carrier of many compounds (Guo et al 2014). Because of their ROS scavenging activity, thiol groups of cysteine residues of albumin determine the plasma redox status (Dobrakowski et al 2014).…”
Section: Discussionmentioning
confidence: 99%
“…Albumin is the most abundant plasma protein, which serves to buffer the blood, maintain the osmotic pressure, and as a carrier of many compounds (Guo et al 2014). Because of their ROS scavenging activity, thiol groups of cysteine residues of albumin determine the plasma redox status (Dobrakowski et al 2014).…”
Section: Discussionmentioning
confidence: 99%
“…When BSA-E2 was bonded onto Cu 2 S, it was obvious that the spectrum of Cu 2 S-BSA-E2 bioconjugates (curve c) was a superposition of curve a and curve b. Electrochemical methods are also suitable for investigating the interaction between biological molecules and other materials. 25 Due to the proteins are intrinsically unable to act as redox partners, the combined biological molecules will weaken the electrochemical signals obviously. From ESI Fig.…”
Section: Characterization Of Cu 2 S and Cu 2 S-bsa-e2 Bioconjugatesmentioning
confidence: 99%
“…In metal coordination chemistry, the term complex means a central metal atom or ions surrounded by a set of ligands, a large number of molecules and ions can behave as ligands, and a large number of metals ions form complexes [6]. A number of functional groups participate in metal binding in metalloproteins; the side chains of Glu , Tyr, Cys, His Arg, Lys, Asp and Met and although free cysteines can potentially bind chelated metals, in practice they are rarely available in the appropriate reduced state [7].In new dimension of protein separations, the apparent affinity of a protein for a metal chelate depends strongly on the metal ion involved in coordination. Protein retention on different metal mirrors the affinity of the metal for imidazole.…”
Section: Introductionmentioning
confidence: 99%
“…Protein retention on different metal mirrors the affinity of the metal for imidazole. The stability constant for complexation with imidazole follows the order Cu 2+ > Zn 2+ and also depends on the quantity of protein that can be loaded onto a given metal-chelate support [7]. Immobilized metal ion chromatography (IMAC) was used to purify protein by using metal binding concept, Ueda et al, (2003).…”
Section: Introductionmentioning
confidence: 99%