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机构地区:[1]清华大学生物科学与技术系生物膜与膜生物工程国家重点实验室
出 处:《生物物理学报》1996年第3期389-393,共5页Acta Biophysica Sinica
基 金:国家自然科学基金
摘 要:研究了轻稀土离子(Ln3+)对钙调蛋白(CaM)调控的磷酸二酯酶(PDE)活力的影响。结果表明,在无Ca2+的CaM(Apo—CaM)体系中,由CaM调节的PDE的活力随Ln3+浓度的变化曲线是双相效应,即在高浓度时,Ln3+具有抑制CaM调节PDE活力的能力;低浓度的Ln3+可以提高CaM调节PDE活力的能力。在Ca2+4-CaM-PDE体系中,高浓度的Ln3+的加入能抑制ChM调节PDE活力的能力,其抑制程度因其离子不同而异。CaM的两类拮抗剂JuA(非竞争性抑制剂)和TFP(竞争性抑制剂)都能抑制CaM-Ln3+-PDE系统的活性。最后对Ln3+和CaM相互作用的分子机制进行了初步的讨论。The effects of light rare earth ions (Ln3+) on the activity of phosphodiesterase (PDE) stimulated by calmodulin (CaM) have been studied. The results revealed that the curve of PDE activeity stimulated by CaM(in absence Ch2+) in different Ln3+ concentration is aparently biphase.Ln3+ can activate CaM almost as same as Ca2+ at low concentration, but they have strongly inhibitive function at high concentration. In addition, Ln3+ at high concentration can inhibit the activity of PDE stimulated by CaM (in presence of Ca2+) and the inhibition effect is dependent on the different ions. Two types of inhibition: trifluopenazine (TEP, a competitive inhibitor of CaM) and jujubosideA (JuA, a non-competitive inhibitor of CaM) can inhibit the activity of PDE stimulated by Ln-CaM. The mechanism of molecular interaction between Ln3+ and CaM has been discussed.
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