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内蒙古自治区呼和浩特市赛罕区大学西街235号 邮编: 010021
作者机构:ECOLE NATL SUPER CHIM EQUIPE RECH CNRS 62 F-34075 MONTPELLIER FRANCE
出 版 物:《BIOCHIMIE》 (Biochimie)
年 卷 期:1976年第58卷第5期
页 面:593-599页
核心收录:
学科分类:0710[理学-生物学] 071010[理学-生物化学与分子生物学] 081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术]
摘 要:The kinetic study of the (Ca2+) ATPase activity of lymphocyte plasma membranes allowed some properties of this enzyme to be evidenced. The Ca2+-activated hydrolysis of ATP is independent of a non-specific alkaline phosphatase. The substrate of the ATPase activity is the chelate Ca2+-ATP. Mg2+ may substitute for Ca2+ both as chelating ion and as activating ion. There is apparently only 1 ATPase, activated either by Ca2+, or by Mg2+ with less efficiency. Both chelates have the same Km;pH values for maximum activity and transition temperatures are identical. The effects of free ions are also the same, activation at low concentration and inhibition at high concentration.