Purification of the Ca2+-stimulated ATPase activator from human erythrocytes. Its membership in the class of Ca2+-binding modulator proteins.
Purification of the Ca2+-stimulated ATPase activator from human erythrocytes. Its membership in the class of Ca2+-binding modulator proteins.
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从人红细胞中纯化 Ca2 刺激的 ATP 酶激活剂。
DOI：
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发表时间：
1978
影响因子：
4.8
通讯作者：
J. T. Penniston
中科院分区：
文献类型：
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作者：
H. Jarrett;J. T. Penniston
从人红细胞中纯化了13，000倍的红细胞膜Ca 2+刺激ATP酶的激活剂。该蛋白在有和无去污剂的电泳和等电聚焦后均呈现单一条带。该蛋白质与牛脑和大鼠睾丸中的Ca 2+结合调节蛋白进行了比较。所有这三种蛋白质是均匀的，共迁移电泳在洗涤剂的存在下，没有洗涤剂在pH值的蛋白质的等电点的两侧。这三种蛋白质的氨基酸组成几乎难以区分，并且所有三种蛋白质都含有1个不寻常的氨基酸三甲基赖氨酸残基。所有这三个也是不可区分的，因为它们的能力，以进一步刺激钙离子刺激的ATP酶的人红细胞膜。因此，我们得出结论，它们代表功能相同的蛋白质。所有三种蛋白质储存后，第二条带可通过洗涤剂凝胶电泳检测到;生化活性和非洗涤剂凝胶上的行为没有改变。这第二条带的存在可能是负责大鼠睾丸和牛脑调节蛋白之间的差异以前的报告。讨论了该蛋白可能是一种通用的细胞内Ca ~（2+）受体，作为细胞内信使介导Ca ~（2+）的活性。
The activator of the Ca2+-stimulated ATPase of erythrocyte membranes was purified 13,000-fold to homogeneity from human erythrocytes. The protein gave a single band upon electrophoresis both with and without detergent, and upon isoelectric focusing. This protein was compared with Ca2+-binding modulator proteins from bovine brain and rat testis. All three proteins were homogeneous and co-migrated on electrophoresis both in the presence of detergent and without detergent at pH values on both sides of the isoelectric point of the protein. The amino acid compositions of the three proteins were nearly indistinguishable, and all three proteins contained 1 residue of the unusual amino acid, trimethyllysine. All three were also indistinguishable as measured by their ability to further stimulate the Ca2+-stimulated ATPase of human erythrocyte membranes. Thus, we conclude that they represent functionally the same protein. Upon storage of all three proteins, a second band was detectable by detergent gel electrophoresis; the biochemical activity and the behavior on nondetergent gels were not changed. The presence of this second band is probably responsible for previous reports of differences between the rat testis and bovine brain modulator protein. The possibility is discussed that this protein is a general intracellular Ca2+ receptor, which mediates the activities of Ca2+ as an intracellular messenger.