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本文研究了山莨菪碱对肌质网Ca~(2+)-ATPase活力及转运功能的影响.对膜结合及分离纯化的Ca~(2+)-ATPase,体系中加入不同量的药物都对酶的活力及转运效率无明显影响.当将药物与肌质网或纯化的Ca~(2+)-ATPase预保温后,山莨菪碱则表现出在低浓度使酶激活,高浓度抑制酶的活力.但都导致SRCa~(2+)转运效率降低.对用保温,超声及去污剂透析三种不同方法重建的脂酶体,结果表明:山莨菪碱通过作用于膜脂后,在低浓度激活Ca~(2+)-ATPase、高浓度抑制酶的活力.比较药物对不同类型纯磷脂重建的脂酶体活性的影响发现:山莨菪碱对含有酸性磷脂的脂酶体Ca~(2+)-ATPase的作用较不含酸性磷脂的要大.
In this paper, we investigated the effect of anisodamin on the Ca ~ (2 +) - ATPase activity and transport function of sarcoplasmic reticulum.For the membrane bound and isolated and purified Ca ~ (2 +) - ATPase, different amounts of drug were added into the system Enzyme activity and transport efficiency had no significant effect.When the drug and sarcoplasmic reticulum or purified Ca ~ (2 +) - ATPase pre-incubated, anisodamine is shown in the low concentration of enzyme activation, high concentration of inhibitory enzyme But all lead to the decrease of SRCa ~ (2+) transport efficiency.The results of three different methods of reconstructing liposomes by heat-preservation, ultrasonography and detergent showed that anisodamine could reduce the transport of SRCa 2+ Concentration of Ca ~ (2 +) - ATPase inhibited the activity of the enzyme.Comparison of the effects of drugs on the activity of liposomes reconstructed with different types of pure phospholipids found that anisodamine inhibited the activity of Ca ~ (2) +) - ATPase than the role of acid phosphatides.