Characterization of the calcium-binding contractile protein centrin from Tetraselmis striata (Pleurastrophyceae).
Characterization of the calcium-binding contractile protein centrin from Tetraselmis striata (Pleurastrophyceae).
复制标题
Tetraselmis striata（侧藻纲）钙结合收缩蛋白中心蛋白的表征。
DOI：
10.1111/j.1550-7408.1992.tb01468.x
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发表时间：
1992
期刊：
影响因子：
--
通讯作者：
Salisbury,JL
中科院分区：
文献类型：
--
作者：
Coling,DE;Salisbury,JL
中心蛋白是绿色四藻（Tetraselmis striata）鞭毛根的主要蛋白质。我们提出了一个新的修改程序，准备足够的数量和纯度的中心蛋白，以允许详细的生化表征。我们确定，通过不同溶解度纯化的中心蛋白，然后通过苯基琼脂糖和DEAE-Sephacel色谱法与直接从条纹鞭毛根中提取的蛋白质在分子量、等电点和SDS-PAGE中的钙依赖性行为方面相同。我们还比较了纯化的中心蛋白的生化性质与钙调素分离的Tetraselmisand钙调素分离的哺乳动物脑。根据分子量、等电点、SDS-PAGE中的钙依赖性行为、蛋白水解肽图谱、氨基酸组成、激活牛脑磷酸二酯酶的能力以及与特异性抗体的反应性，中心蛋白可以与藻类或哺乳动物钙调蛋白完全区分开。
Centrin is a major protein of the contactile striated flagellar roots of the green algaTetraselmis striata. We present a newly modified procedure for the preparation of centrin in sufficient quantity and purity to allow for detailed biochemical characterization. We establish that centrin purified by differential solubility, followed by phenyl‐Sepharose and DEAE‐Sephacel chromatography is identical with the protein extracted directly from striated flagellar roots with regard to molecular weight, isoelectric point, and calcium‐dependent behavior in SDS‐PAGE. We also compare the biochemical properties of purified centrin with calmodulin isolated fromTetraselmisand calmodulin isolated from mammalian brain. Centrin can be fully distinguished from either algal or mammalian calmodulin on the basis of molecular weight, isoelectric point, calcium‐dependent behavior in SDS‐PAGE, proteolytic peptide maps, amino acid composition, ability to activate bovine brain phosphodiesterase, and reactivity with specific antibodies.