Two New Copper Proteins from Human Brain Isolation and Properties*

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Abstract
1. Two new copper proteins (albocuprein I and II) have been isolated from human brain. Highly purified by disc electrophoresis, gel filtration and ultracentrifugation, albocuprein I and II are pale yellow proteins with molecular weights of 72, 000±2, 000 and 14, 000±500, respectively, as estimated by gel filtration. 2. The copper content of albocuprein I was 0.25±0.05%, in which 35±15% was accounted for by cupric copper, as estimated by Electron Spin Resonance (ESR), with gm=2.06±0.005, g‖=2.28±0.005, and A‖=(158±10)× 10−4cm−1. Albocuprein II had a specific copper concentration of 1.4±0.1%, and gave no ESR signals. Absorption spectra showed no maxima in the vicinity of 600 mμ, nor were detected enzymatic activities with either protein. 3. A possible relationship of albocuprein I to ceruloplasmin is noted in view of the observation that the antibody to albocuprein I decreased the oxidative activity of ceruloplasmin by 55% or more, and changed the ESR signal pattern of ceruloplasmin, although it did not precipitate the latter protein. 4. Single precipitin bands were found between albocuprein I antibody and extracts of cerebrum, cerebellum, basal ganglia, pons, spinal cord, peripheral nerve, heart and kidney.

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