Purification of calcium-dependent phosphodiesterases from rat cerebrum by affinity chromatography on activator protein-sepharose. |
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| Authors: | M Miyake J W Daly C R Creveling |
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| Institution: | National Institute of Arthritis, Metabolism, and Digestive Diseases, National Institutes of Health, Bethesda, Maryland 20014 U.S.A. |
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| Abstract: | Calcium-dependent activator protein purified from rat cerebrum was reacted with either N-hydroxysuccinimide-activated succinylated aminopropyl agarose or cyanogen bromide-activated Sepharose 4B. The activator protein-agarose column did not serve as an affinity adsorbant for purification of calcium-dependent phosphodiesterases from rat brain. The activator protein-Sepharose was an effective adsorbant for calcium-dependent phosphodiesterases. In the presence of calcium ions, this column selectively retained the calcium-dependent phosphodiesterases from soluble and solubilized particulate fractions from rat cerebrum. The phosphodiesterases were eluted from the column in the presence of ethylenebis(oxyethylenenitrilo)]tetraacetic acid. |
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