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- W2024773012 abstract "Abstract Cyclic nucleotide phosphodiesterase was purified over 200-fold in a single step from the rat heart cytosolic fraction, using affinity chromatography on phenylbutenolide inhibitor immobilized to AH Sepharose. After elimination of the contaminating proteins by washing with the loading buffer and then with 0.4 M KCl buffer, without any loss in enzymatic activity, the cyclic nucleotide phosphodiesterase was eluted in good zields with a linear KCl gradient from 0.4 M to 1.8 M. Enzymatic activity determination performed with both cyclic AMP and cyclic GMP as substrate, either at low (0.25 μM) or at high (25 μM) concentration, pointed out the presence of several phosphodiesterase forms with different substrate specificities, in the elution profiles." @default.
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- W2024773012 date "1980-08-01" @default.
- W2024773012 modified "2023-10-16" @default.
- W2024773012 title "Purification of rat heart cyclic nucleotide phosphodiesterase on column of immobilized phenylbutenolide inhibitor" @default.
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- W2024773012 doi "https://doi.org/10.1016/0006-291x(80)91583-1" @default.
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