Journal ArticleDOI
Cadmium(II), zinc(II), and copper(II) ions binding to bovine serum albumin. A 113Cd NMR study
TLDR
Competition between Zn(II) (or Cu(II)) and Cd( II) for the strong sites indicates that there is a common strong binding site for Cu( II), Zn (II) andCd(II), with higher affinity for Cu-II and Zn-II than for C d(II).About:
This article is published in Inorganica Chimica Acta.The article was published on 1982-01-01. It has received 57 citations till now. The article focuses on the topics: Bovine serum albumin.read more
Citations
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Journal ArticleDOI
Binding of transition metal ions to albumin: sites, affinities and rates.
TL;DR: The thorough understanding of metal binding properties of serum albumin, including the competition of various metal ions for specific binding sites is important for biomedical issues, such as new disease markers and design of metal-based drugs.
Journal ArticleDOI
Multi-metal binding site of serum albumin.
TL;DR: In this article, the second specific metal binding site on human, bovine and porcine albumins Ni(II, Zn(II), Cd(II) was investigated using electron spin resonance spectroscopy.
Journal ArticleDOI
113Cd NMR spectroscopy of coordination compounds and proteins
TL;DR: In this article, it was shown that ligand atom type and number, bond lengths, coordination geometry, and neighboring atoms (including other metals) all influence 113Cd chemical shifts.
Journal ArticleDOI
Albumin as a zinc carrier: properties of its high-affinity zinc-binding site
TL;DR: Comparisons of X-ray crystal structures of free and fatty-acid bound human serum albumin suggest that zinc binding to this site and fatty acid binding to one of the five major sites may be interdependent, and interactive binding of zinc and long-chain fatty acids to albumin may have physiological implications.
Journal ArticleDOI
Highly reactive trans-cyclooctene tags with improved stability for Diels-Alder chemistry in living systems.
Raffaella Rossin,Sandra M. van den Bosch,Wolter ten Hoeve,M Marco Carvelli,Ron M. Versteegen,Johan Lub,Marc S. Robillard +6 more
TL;DR: The reactivity of the fastest bioorthogonal reaction, the inverse-electron-demand-Diels-Alder cycloaddition between a tetrazine probe and a trans-cyclooctene-tagged antibody, can be increased 10-fold, approaching the speed of biological interactions, while also increasing its stability.
References
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Journal ArticleDOI
Complete amino acid sequence of human serum albumin.
TL;DR: This paper reports on the complete amino acid sequence of human serum albumin, including the positions of all amides; the results presented are confronted with sequential data reported from other laboratories.
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Copper-binding Properties of Bovine Serum Albumin and Its Amino-terminal Peptide Fragment
TL;DR: Spectral and titrimetric data are reported which suggest that the Cu(II)-binding site for both albumin and peptide is a chelate locus involving multiple nitrogenous ligands in the neutral pH range, and that a histidyl residue occupies position 3 in the peptide chain.
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A fluorescence stopped flow analysis of Ca2+ exchange with troponin C.
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A Peptide Molecule Mimicking the Copper(II) Transport Site of Human Serum Albumin A COMPARATIVE STUDY BETWEEN THE SYNTHETIC SITE AND ALBUMIN
TL;DR: The interaction of peptide with Cu(II) in the presence of albumin, studied by equilibrium dialysis at pH 7.53 and ionic strength 0.16, indicates that this tripeptide is able to compete with albumin for Cu( II), and the biomedical implications of designing a small molecule to mimic certain functions of a biologically important macromolecule are discussed.