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钙调蛋白(calmodulin,CaM)作为环核苷酸磷酸二酯酸(PDE)的内源性活化因子,于六十年代后期由张怀耀首先发现,它是细胞内Ca~(2+)的重要受体,与Ca~(2+)结合后发生构象变化而激活,又调节着细胞内Ca~(2+)的浓度。它不具有酶的活性,却能通过激活细胞内广泛的酶谱,调控细胞的基本功能。二价阳离子竞争性地取代Ca~(2+)的结合后能影响CaM活性,组织内还存在有CaM的内源性抑制因子,竞争性地与CaM结合而抑制CaM的活性。CaM与靶酶的相互作用也能被很多药物所抑制,这或许与药物的作用机制有关。
Calmodulin (CaM), as the endogenous activating factor of cyclic nucleotide phosphodiester acid (PDE), was first discovered by Zhang Huaiyao in the late 1960’s as an important receptor for intracellular Ca 2+ The body, with Ca ~ (2+) combined with the conformational changes and activation, but also regulate the intracellular Ca ~ (2+) concentration. It does not have enzyme activity, but it can regulate the basic function of cells by activating a wide range of enzymes in the cell. Divalent cations competitively replace Ca ~ (2+) binding can affect the activity of CaM, there is also an endogenous inhibitor of CaM in the tissue, competitively binding to CaM and inhibiting the activity of CaM. The interaction between CaM and target enzyme can also be inhibited by many drugs, which may be related to the mechanism of action of drugs.