Carraway C A, Corrado F J, Fogle D D, Carraway K L
Biochem J. 1980 Oct 1;191(1):45-51. doi: 10.1042/bj1910045.
Intact viable 13762 mammary-adenocarcinoma ascites cells hydrolyse added ATP. The localization of hydrolysis product and inactivation by the slowly penetrating chemical reagent diazotized sulphanilic acid indicate that this ATPase is at the external surface of the cell. A number of features differentiate this enzyme from mitochondrial, myosin and cation-transport ATPases. It is stimulated by either Ca2+ or Mg2+ and has little or no activity in their absence. It is insensitive to ouabain, oligomycin and azide. It is the major ATPase activity found in homogenates of gently disrupted 13762 cels. The ATPase activity is inhibited at high substrate concentrations and shows an apparent stimulation by concanavalin A in isolated membranes, but not in intact cells. The stimulation by concanavalin A results predominantly from a release from substrate inhibition.
完整存活的13762乳腺腺癌细胞腹水细胞能水解添加的ATP。水解产物的定位以及缓慢渗透的化学试剂重氮化磺胺酸的失活表明，这种ATP酶位于细胞外表面。该酶在多个方面与线粒体、肌球蛋白和阳离子转运ATP酶不同。它受Ca2+或Mg2+刺激，在缺乏它们时活性很小或没有活性。它对哇巴因、寡霉素和叠氮化物不敏感。它是轻度破碎的13762细胞匀浆中发现的主要ATP酶活性。ATP酶活性在高底物浓度下受到抑制，在分离的膜中，伴刀豆球蛋白A对其有明显刺激作用，但在完整细胞中则没有。伴刀豆球蛋白A的刺激主要是由于底物抑制的解除。
