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• W1987502009 abstract "Abstract The phosphodiesterase activities of the 15-day-old embryonic chick ovary have been investigated. Kinetic analysis of the embryonic ovarian cyclic AMP phosphodiesterase activity by Lineweaver-Burk double-reciprocal plot demonstrated two enzymatic activities. The apparent K m value for the high-affinity enzyme was 4.0 μ M with a V max of 1.56 nmol/mg protein/min whereas the apparent K m of the low-affinity enzyme was 37 μ M with a V max of 10.0 nmol/mg protein/min. Kinetic analysis of cyclic GMP hydrolysis indicated a single enzyme activity with an apparent K m value of 8.3 μ M and a V max of 8 nmol/mg protein/min. The hydrolysis of cyclic GMP, but not cyclic AMP, was inhibited by EGTA. The inhibition of cyclic GMP hydrolysis caused by EGTA can be relieved by the addition of exogenous Ca 2+ . 3-Isobutyl-1-methylxanthine at 100 μ M concentration inhibited both cyclic AMP and cyclic GMP hydrolysis to 50% of their original activity. In the developing ovary, the cyclic GMP phosphodiesterase activity remained constant, while the cyclic AMP phosphodiesterase activity was higher in the earlier stages as compared to the later stages. The enzyme kinetic behaviors of ovarian cyclic AMP and cyclic GMP phosphodiesterase were unchanged in all embryonic stages investigated." @default.
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• W1987502009 date "1981-08-01" @default.
• W1987502009 modified "2023-10-17" @default.
• W1987502009 title "Cyclic nucleotide phosphodiesterase activities of the embryonic chick ovary" @default.
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• W1987502009 doi "https://doi.org/10.1016/0016-6480(81)90327-0" @default.
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