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.
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.