Purification and biochemical properties of calmodulin from Saccharomyces cerevisiae.
Purification and biochemical properties of calmodulin from Saccharomyces cerevisiae.
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酿酒酵母钙调蛋白的纯化和生化特性。
DOI：
10.1111/j.1432-1033.1987.tb13380.x
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发表时间：
1987
期刊：
影响因子：
--
通讯作者：
Y. Anraku
中科院分区：
文献类型：
--
作者：
Y. Ohya;I. Uno;T. Ishikawa;Y. Anraku
通过疏水相互作用层析和高效液相凝胶过滤，从酿酒酵母中分离纯化出完全均一的钙调蛋白。在不同的标准下对纯化的蛋白作为钙调蛋白的生化性质进行了检测，并描述了它与其他钙调蛋白的相似性和差异性。与其他钙调蛋白一样，酵母钙调素对牛磷酸二酯酶和豌豆NAD激酶的激活依赖于钙离子，但其半最大激活浓度是牛钙调素的8-10倍。酵母钙调蛋白的氨基酸组成不同于其他低等真核生物的钙调蛋白，它不含酪氨酸，但含有较多的亮氨酸，并具有较高的丝氨酸/苏氨酸比率。酵母钙调素不含色氨基和酪氨酸残基，其紫外光谱反映了苯丙氨基残基的吸光度，在259 nm处的摩尔吸收系数为1900M-1 cm-1。与对其他钙调蛋白的影响不同，钙离子改变了酵母钙调素的二级结构，导致α-螺旋含量下降3%。抗酵母钙调素抗体与牛钙调素无交叉反应，抗牛钙调素抗体与酵母钙调素无交叉反应，可能是由于抗原点氨基酸序列不同所致。结果表明，酵母钙调素的分子结构不同于其他来源的钙调素，但其钙依赖的调节功能高度保守，与高等真核生物的钙调蛋白基本相似。
Calmodulin from the yeast Saccharomyces cerevisiae was purified to complete homogeneity by hydrophobic interaction chromatography and HPLC gel filtration. The biochemical properties of the purified protein as calmodulin were examined under various criteria and its similarity and dissimilarity to other calmodulins have been described. Like other calmodulins, yeast calmodulin activated bovine phosphodiesterase and pea NAD kinase in a Ca2+-dependent manner, but its concentration for half-maximal activation was 8-10 times that of bovine calmodulin. The amino acid composition of yeast calmodulin was different from those of calmodulins from other lower eukaryotes in that it contained no tyrosine, but more leucine and had a high ratio of serine to threonine. Yeast calmodulin did not contain tryptophanyl or tyrosyl residues, so its ultraviolet spectrum reflected the absorbance of phenylalanyl residues, and had a molar absorption coefficient at 259 nm of 1900 M-1 cm-1. Ca2+ ions changed the secondary structure of yeast calmodulin, causing a 3% decrease in the alpha-helical content, unlike its effect on other calmodulins. Antibody against yeast calmodulin did not cross-react with bovine calmodulin, and antibody against bovine calmodulin did not cross-react with yeast calmodulin, presumably due to differences in the amino acid sequences of the antigenic sites. It is concluded that the molecular structure of yeast calmodulin differs from those of calmodulins from other sources, but that its Ca2+-dependent regulatory functions are highly conserved and essentially similar to those of calmodulins of higher eukaryotes.
来自盘基网柄菌的新型钙调蛋白的表征。
DOI：
--
发表时间：
1981
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Bazari,WL;Clarke,M
通讯作者：
Clarke,M
抗脊椎动物钙调蛋白抗血清的可重复生产和免疫反应位点的测定。
DOI：
--
发表时间：
1981
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
VanEldik,LJ;Watterson,DM
通讯作者：
Watterson,DM
菠菜钙调蛋白：分离、表征以及与脊椎动物钙调蛋白的比较。
影响因子：
2.9
作者：
Watterson,DM;Iverson,DB;VanEldik,LJ
通讯作者：
VanEldik,LJ