Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.16.3.1 (ceruloplasmin)
 5,074 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Nanogold particles of size 15 nm were used to label goat anti-human ceruloplasmin (GCP) to obtain an immunonanogold probe (AuGCP) for ceruloplasmin (CP). In a pH 7.8 citric acid-Na(2)HPO(4) buffer solution and in the presence of polyethylene glycol (PEG), an immunoreaction between AuGCP and CP took place, and the released nanogold particles aggregated to bigger clusters, which caused the resonance scattering (RS) intensity at 552 nm (I(552nm)) to be enhanced greatly. The enhanced intensity DeltaI was proportional to the CP concentration (C(CP)) in the range from 0.0030 to 1.26 microg/mL, with a regress equation of DeltaI = 101.0C(CP) + 1.8, a correlation coefficient of 0.9970, and a detection limit of 1.1 ng/mL CP. This simple and sensitive RS immunoassay was applied to the determination of CP in human plasma, with satisfactory results.
 ...
PMID:Rapid assay of trace ceruloplasmin using an immunonanogold resonance scattering spectral probe. 1935 83

Bacterioferritin (Bfr) is a spherical protein composed of 24 subunits and 12 heme molecules. Bfrs contribute to regulate iron homeostasis in bacteria by capturing soluble but potentially toxic Fe(2+) and by compartmentalizing it in the form of a bioavailable ferric mineral inside the protein's hollow cavity. When iron is needed, Fe(3+) is reduced and mobilized into the cytosol as Fe(2+). Hence, key to the function of Bfr is its ability to permeate iron ions in and out of its interior cavity, which is likely imparted by a flexible protein shell. To examine the conformational flexibility of Bfrs in a native-like environment and the way in which the protein shell interacts with monovalent cations, we have performed molecular dynamics (MD) simulations of BfrB from Pseudomonas aeruginosa (Pa BfrB) in K(2)HPO(4) solutions at different ionic strengths. The results indicate the presence of coupled thermal fluctuations (dynamics) in the 4-fold pores and B-pores of the protein, which is key to allowing passage of monovalent cations through the protein shell using B-pores as conduits. The MD simulations also show that Pa BfrB ferroxidase centers are highly dynamic and permanently populated by transient cations exchanging with other cations in the interior cavity, as well as the solution bathing the protein. Taken together, the findings suggest that Fe(2+) passes across the Pa BfrB shell via B-pores and that the ferroxidase pores allow the capture and oxidation of Fe(2+), followed by translocation of Fe(3+) to the interior cavity, aided by the conformationally active H130.
 ...
PMID:Protein dynamics and ion traffic in bacterioferritin. 2316 35