红细胞膜片段中钙离子的主动摄取以及钙激活的镁离子ATP酶
Active uptake of Ca++ and Ca plus,plus-activated Mg++ ATPase in red cell membrane fragments.
作者信息
Cha Y N, Shin B C, Lee K S
出版信息
J Gen Physiol. 1971 Feb;57(2):202-15. doi: 10.1085/jgp.57.2.202.
Isolated human red blood cell membrane fragments (RBCMF) were found to take up Ca(++) in the presence of ATP.(1) This ATP-dependent Ca(++) uptake by RBCMF appears to be the manifestation of an active Ca(++) transport mechanism in the red cell membrane reported previously (Schatzmann, 1966; Lee and Shin, 1969). The influences of altering experimental conditions on Ca(++)-stimulated Mg(++) ATPase (Ca(++) ATPase) and Ca(++) uptake of RBCMF were studied. It was found that pretreatment of RBCMF at 50 degrees C abolished both Ca(++) ATPase and Ca(++) uptake. Pretreatment of RBCMF with phospholipases A and C decreased both Ca(++) ATPase and Ca(++) uptake, whereas pretreatment with phospholipase D did not significantly alter either Ca(++) ATPase or Ca(++) uptake. Both Ca(++) ATPase and Ca(++) uptake had ATP specificity, similar optimum pH's, and optimum incubation temperatures. From these results, it was concluded that Ca(++) uptake is intimately linked to Ca(++) ATPase.
在ATP存在的情况下，发现分离的人红细胞膜碎片（RBCMF）能摄取Ca(++)。(1) RBCMF的这种ATP依赖性Ca(++)摄取似乎是先前报道的红细胞膜中一种活性Ca(++)转运机制的表现（Schatzmann，1966年；Lee和Shin，1969年）。研究了改变实验条件对Ca(++)刺激的Mg(++) ATP酶（Ca(++) ATP酶）和RBCMF的Ca(++)摄取的影响。发现将RBCMF在50摄氏度下预处理会消除Ca(++) ATP酶和Ca(++)摄取。用磷脂酶A和C预处理RBCMF会降低Ca(++) ATP酶和Ca(++)摄取，而用磷脂酶D预处理则不会显著改变Ca(++) ATP酶或Ca(++)摄取。Ca(++) ATP酶和Ca(++)摄取都具有ATP特异性、相似的最佳pH值和最佳孵育温度。从这些结果得出结论，Ca(++)摄取与Ca(++) ATP酶密切相关。
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