Copper-binding Properties of Bovine Serum Albumin and Its Amino-terminal Peptide Fragment
TLDR
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.About:
This article is published in Journal of Biological Chemistry.The article was published on 1967-04-10 and is currently open access. It has received 199 citations till now. The article focuses on the topics: Bovine serum albumin & Serum albumin.read more
Citations
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Book ChapterDOI
Structure of serum albumin.
Daniel C. Carter,Joseph X. Ho +1 more
TL;DR: This chapter provides an insight of the findings of past significant papers with the current knowledge of the recently determined high resolution X-ray structure of serum albumin and suggests that AFP may have a higher affinity for some unknown ligands important for fetal development.
Journal ArticleDOI
Copper Homeostasis and Neurodegenerative Disorders (Alzheimer's, Prion, and Parkinson's Diseases and Amyotrophic Lateral Sclerosis)
Journal ArticleDOI
The role of oxidized lipoproteins in atherogenesis
TL;DR: Current understanding of the mechanisms of low-density lipoprotein (LDL) oxidation and the potential role of oxidized lipoproteins in atherosclerosis are reviewed and potential strategies for inhibiting oxidation in the vessel wall are suggested.
Journal ArticleDOI
Structural implications derived from the analysis of electron paramagnetic resonance spectra of natural and artificial copper proteins
TL;DR: It is concluded that in artificial copper proteins as well as in the naturally occurring nonblue copper proteins copper is ligated to oxygen and nitrogen but not to sulfur.
Journal ArticleDOI
The Three Recombinant Domains of Human Serum Albumin STRUCTURAL CHARACTERIZATION AND LIGAND BINDING PROPERTIES
TL;DR: A generally applicable purification protocol based on Cibacron Blue affinity chromatography is established, suggesting that each of the three domains of human serum albumin carries a binding site specific for this ligand.
References
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Journal ArticleDOI
Reactivity of sperm whale metmyoglobin towards hydrogen ions and p-nitrophenyl acetate.
TL;DR: The first of a projected series of studies addressed to these closely related questions is presented in this article, where the authors studied the equilibria of metmyoglobin with hydrogen ions, with greatest emphasis on the pH range below 9.
Journal ArticleDOI
Studies on copper metabolism I. A method for the determination of copper in whole blood, red blood cells, and plasma.
Journal ArticleDOI
Isolation of Two Large Peptide Fragments from the Amino- and Carboxyl-terminal Positions of Bovine Serum Albumin
Theodore Peters,Cynthia Hawn +1 more
TL;DR: Evidence is presented that these preparations, termed the "Asp" and "Phe" fragments include the two terminal sites of the albumin molecule, and the presence of 3 histidine residues and of the free terminal amino group suggests a role in binding small compounds.
Related Papers (5)
Ternary Coordination Complex between Human Serum Albumin, Copper (II), and l-Histidine
Show-Jy Lau,Bibudhendra Sarkar +1 more