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有证据表明,来自牛腮腺富含质膜部分的Ca(2+)-ATP酶和(Ca2+ + Mg2+)-ATP酶活性存在于同一酶分子上。

Evidence that both Ca(2+)-ATPase and (Ca2+ + Mg2+)-ATPase activities in the plasma membrane-rich fraction from bovine parotid gland reside on the same enzyme molecule.

作者信息

Matsukawa R, Hayakawa M, Araya M, Imamura T, Takiguchi H

机构信息

Department of Biochemistry, Nihon University School of Dentistry at Matsudo, Chiba, Japan.

出版信息

Int J Biochem. 1994 Feb;26(2):287-93. doi: 10.1016/0020-711x(94)90159-7.

Abstract
  1. Evidence was obtained that activities of both low-affinity Ca(2+)-ATPase and high-affinity (Ca2+ + Mg2+)-ATPase in the plasma membrane-rich fraction from bovine parotid gland reside on the same enzyme. 2. Two solubilized ATPases were purified by four steps of HPLC; and both activities eluted at the same fractions from each column, and the specific activity ratio of the two enzymes at each step was constant. 3. By non-denaturing PAGE, the final preparation gave a single band for both protein staining and activity staining for the two ATPases; and the Ca(2+)-ATPase activity comigrated with that of (Ca2+ + Mg2+)-ATPase. 4. In SDS-PAGE, each activity staining for the ATPases also gave a single band, and both activities comigrated. 5. These findings suggest that Ca(2+)-ATPase and (Ca2+ + Mg2+)-ATPase are a single enzyme.
摘要
  1. 有证据表明,牛腮腺富含质膜部分中的低亲和力Ca(2+)-ATP酶和高亲和力(Ca2+ + Mg2+)-ATP酶的活性存在于同一种酶上。2. 两种可溶的ATP酶通过高效液相色谱的四个步骤进行纯化;两种活性在每根柱子的相同馏分中洗脱,并且在每个步骤中两种酶的比活性比是恒定的。3. 通过非变性聚丙烯酰胺凝胶电泳,最终制剂对两种ATP酶的蛋白质染色和活性染色均呈现单一条带;并且Ca(2+)-ATP酶活性与(Ca2+ + Mg2+)-ATP酶活性迁移在一起。4. 在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳中,ATP酶的每种活性染色也呈现单一条带,并且两种活性迁移在一起。5. 这些发现表明Ca(2+)-ATP酶和(Ca2+ + Mg2+)-ATP酶是同一种酶。

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