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)

The conformational features of copper-free ceruloplasmin (CP), as compared to the holo-protein, were evaluated utilizing far- and near-UV circular dichroism and fluorescence spectroscopy. The results obtained indicate that apo-CP maintains the secondary structure of the holo-protein, while the tertiary interactions are much weaker. In addition, the removal of copper from the holo-protein leads to the exposure of hydrophobic patches to solvent, as shown by the fact that apo-CP, at variance from the holo-protein, binds the hydrophobic probe ANS. It is proposed that the CP molecule, upon copper removal, acquires the conformational features typical of a molten globule, which might be the conformational state of CP during its biosynthesis before metal incorporation.
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PMID:Evidence for the molten globule state of human apo-ceruloplasmin. 891 11