Allende C, Plaza M
Departamento de Biologia, Facultad de Ciencias, Universidad de Chile, Santiago.
Comp Biochem Physiol B. 1987;88(2):581-7. doi: 10.1016/0305-0491(87)90348-8.
A cGMP-stimulated cyclic nucleotide phosphodiesterase present in cytosol of Xenopus laevis ovary has been purified and characterized. A cAMP-specific phosphodiesterase which is not activated by either cGMP or calmodulin, has also been characterized. Brief exposure of intact oocytes to 10 micro M progesterone results in an increase in activity of the cAMP-specific enzyme. The cGMP-stimulated and the calmodulin-activated phosphodiesterases are not altered. Changes in cyclic nucleotide levels during progesterone-induced maturation of oocytes may be modulated by these isoenzymes.
一种存在于非洲爪蟾卵巢细胞质中的受环磷酸鸟苷（cGMP）刺激的环核苷酸磷酸二酯酶已被纯化并进行了特性分析。还对一种既不受cGMP也不受钙调蛋白激活的cAMP特异性磷酸二酯酶进行了特性分析。将完整的卵母细胞短暂暴露于10微摩尔的孕酮中会导致cAMP特异性酶的活性增加。而受cGMP刺激的和受钙调蛋白激活的磷酸二酯酶则没有变化。在孕酮诱导的卵母细胞成熟过程中环核苷酸水平的变化可能受这些同工酶的调节。
