Breitbart H, Rubinstein S
Arch Androl. 1982 Sep;9(2):147-57. doi: 10.3109/01485018208990233.
The activity of divalent cation-stimulated adenosine triphosphatase (ATPase) has been studied in vesicular membranes isolated from ejaculated ram seminal plasma. This nonspecific acidic ATPase can be activated by millimolar concentration of any one of the following cations: Ca2+, Mg2+, Zn2+, or Mn2+ to give high specific activity (approximately 300 mumol/mg/hr), in absence of the other cations. Free Zn2+ inhibits activity of this ATPase. The Km for adenosonine triphosphate (ATP) ranged between 0.17 and 0.24 mM, and for the divalent cation ranged between 0.4 and 0.8 mM. When the ATPase is activated by Ca2+, two Kms for Ca2+ concentration were found: 0.8 and 0.08 mM. It is suggested that the seminal plasma membranes also contain alkaline ATPase, which is more specific for Ca2+.
对从射精公羊精浆中分离出的囊泡膜中二价阳离子刺激的三磷酸腺苷酶（ATP酶）活性进行了研究。这种非特异性酸性ATP酶可被以下任何一种阳离子的毫摩尔浓度激活：Ca2+、Mg2+、Zn2+或Mn2+，在不存在其他阳离子的情况下产生高比活性（约300 μmol/mg/小时）。游离Zn2+抑制这种ATP酶的活性。三磷酸腺苷（ATP）的米氏常数（Km）在0.17至0.24 mM之间，二价阳离子的Km在0.4至0.8 mM之间。当ATP酶被Ca2+激活时，发现了两个Ca2+浓度的Km：0.8和0.08 mM。有人提出，精浆膜中还含有碱性ATP酶，它对Ca2+更具特异性。
