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Journal ArticleDOI

A kinetic study on the distribution of Cu(II)-ions between albumin and transferrin

Rolf A. Løvstad
- 01 Apr 2004 - 
- Vol. 17, Iss: 2, pp 111-113
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TLDR
The present study shows that both human- and bovine albumin could take up part of the transferrin bound Cu(II), the second order rate constant for the reaction estimated to 12 mM−1 min−1 for both species.
Abstract
Serum albumin (human, bovine) has a specific Cu(II)-ion binding site, and is proposed to act as a copper transport protein in blood plasma. Human transferrin, normally about 30% saturated with iron in vivo, has two sites/molecule capable of complexing Cu(II); one more strongly than the other (Hirose et al. 1996). The present study shows that this binding site has a slightly stronger affinity for Cu(II) than that on the albumins. However, both human- and bovine albumin could take up part of the transferrin bound Cu(II), the second order rate constant for the reaction estimated to 12 mM−1 min−1 for both species. In vivo the albumin concentration is considerably higher than that of iron-free transferrin, and it seems unlikely that the latter can compete with albumin for non-ceruloplasmin cupric ions.

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Citations
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TL;DR: In this paper, the authors highlight the fluorescent chemosensors for metal ions, which have been recently developed from the laboratory of Cai et al. They classify them by target metal ions and introduce various ligands to core fluorophores, such as, rhodamine, fluorescein, pyrene, anthracene, naphthalimide, coumarin, and BODIPY.
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Naphthalimide Modified Rhodamine Derivative: Ratiometric and Selective Fluorescent Sensor for Cu2+ Based on Two Different Approaches

TL;DR: A new rhodamines-based derivative bearing a 1,8-naphthalimide group was synthesized as a dual-mode Cu(2+)-selective sensor via the rhodamine ring-opening approach and ratiometric displacement.
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Encapsulation of strongly fluorescent carbon quantum dots in metal-organic frameworks for enhancing chemical sensing.

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References
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Journal ArticleDOI

Intrinsic stoichiometric equilibrium constants for the binding of zinc(II) and copper(II) to the high affinity site of serum albumin.

TL;DR: Comparison of binding strengths was possible only through the calculation of an intrinsic stoichiometric binding constant and it was suggested that while both histidyl and carboxyl groups appear to be involved in copper binding, Histidyl residues alone were sufficient for zinc binding.
Journal ArticleDOI

Ternary Coordination Complex between Human Serum Albumin, Copper (II), and l-Histidine

TL;DR: Equilibria, existing in the ternary complex system, suggest that the teranary complex may play an important role in the biological transport of Cu(II).
Journal ArticleDOI

Distribution of Copper Among Components of Human Serum

TL;DR: The results showed that, contrary to earlier conclusions, ceruloplasmin copper only comprised about 60% of the total in human serum; and not just cerulplasmin but also other forms of serum copper may be elevated in cancer patients.
Journal ArticleDOI

Metabolism of radiocopper (Cu64) in the rat

TL;DR: Maximal concentrations of Cu64 were reached quickly in the excretory organs—liver, kidney, and gastrointestinal tract—which then slowly released their radioactivity in most of the other organs, suggesting that ceruloplasmin may be the copper donor for the tissues.
Journal ArticleDOI

The intracellular distribution of the radiocopper derived from ceruloplasmin and from albumin.

TL;DR: Within the specific time scales of these experiments the copper from ceruloplasmin becomes the functional, intrinsic copper and that albumin copper becomes the non-functional extraneous copper of cytochrome c oxidase.
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