Kukushkina D M, Cherepnov V L
Biull Eksp Biol Med. 1976 Feb;81(2):171-2.
Adenosine triphosphatase (ATPase) activated by Mg2+ or Ca2+ ions was detected in single mechanoreceptors (Pacini's corpuscles) of cat; addition of Ca2+ (10(-5)M) to Mg-ATP-ase increased the activity by the factor of 1.6. The activity optimum of Mg- or Co-ATPase was in the alkaline pH zone. A high substrate specificity of Mg, Ca-ATPase was shown. Parachlorinemercury-benzoate (5muM) considerably reduced the activity of Mg, Ca-ATPase, whereas oubain (10(-5)M) failed to affect it significantly. It is supposed that Mg, Ca-ATPase of Pacini's corpuscles was close to actomyosine -like proteins.
在猫的单个机械感受器（帕西尼小体）中检测到了由Mg2+或Ca2+离子激活的三磷酸腺苷酶（ATPase）；向Mg-ATP酶中添加Ca2+（10^(-5)M）可使活性提高1.6倍。Mg-或Co-ATP酶的活性最适值处于碱性pH区。显示出Mg, Ca-ATP酶具有较高的底物特异性。对氯汞苯甲酸（5μM）可显著降低Mg, Ca-ATP酶的活性，而哇巴因（10^(-5)M）对其活性没有显著影响。据推测，帕西尼小体的Mg, Ca-ATP酶类似于肌动球蛋白样蛋白。
