Selective modification of the two type I copper sites in human and bovine ceruloplasmin with the action of azide and L-cysteine.
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概要
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The two type I copper sites of human and bovine ceruloplasmin (CP) were indirectly modified through the binding of N<SUB>3</SUB><SUP>−</SUP> to types II and III copper ions. Based on the fact that the activities of CP's modified with N<SUB>3</SUB><SUP>−</SUP> were 85 and 47% for human and bovine CP, respectively, it was disclosed that the electronic and steric states of the "fast" type I Cu or "CuA" which is coupled with the types II and III copper ions was changed reversibly, whilst the "slow" type I Cu or "CuB" which is not coupled with the types II and III copper ions was changed to a type II copper ion and/or irreversibly reduced. On the other hand, the reaction of a limited amount of L-cysteine with CP gave the absorption and electron paramagnetic resonance spectra of CP whose CuB was selectively reduced. The treatment of this CP with 4,7-diphenyl-2,9-dimethyl-1,10-phenanthroline-4′,4″-disulfonate did not result in the selective removal of CuB.
- 公益社団法人 日本化学会の論文
著者
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Sakurai Takeshi
Institute of Chemistry, College of General Education, Osaka University
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Nakahara Akitsugu
Institute Of Chemistry College Of General Education Osaka University
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Sakurai Takeshi
Institute For Molecular Science
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