Zn2+存在下的酸性pH对犬肾BBMV atp酶活性的刺激:一种不同于转运atp酶和碱性磷酸酶的atp酶活性,可能是一种外源性atp酶。

S A Hilden, N E Madias
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引用次数: 4

摘要

犬肾刷状边界膜泡(BBMV)具有至少两种atp酶活性。在本研究中,我们研究了pH、离子和抑制剂对BBMV中atp酶活性的影响。两组不同的条件被确定产生atp酶活性的刺激。在酸性pH下,在1mm ZnCl2的存在下,BBMV atp酶活性发生了独特的刺激。在没有Zn2+的情况下,碱性pH值刺激了第二种atp酶的活性,pH值在8.5 ~ 9.0之间达到峰值。结果表明,碱性ph刺激下ATP的水解可能代表BBMV碱性磷酸酶的活性。独特的酸性pH + Zn2(+)刺激的atp酶活性一定代表了碱性磷酸酶以外的第二种蛋白质的活性,因为纯化的碱性磷酸酶没有显示出这种活性。这种肾BBMV atp酶活性的生化特性和生理功能尚未确定,但可能是一种外泌atp酶。
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Stimulation of canine kidney BBMV ATPase activity by acidic pH in the presence of Zn2+: an ATPase activity distinct from transport ATPases and alkaline phosphatase that may be an ecto-ATPase.

Renal brush border membrane vesicles (BBMV) of the dog possess at least two ATPase activities. In the present study, we have examined the effect of pH, ions, and inhibitors on the activity of ATPase in BBMV. Two different sets of conditions were identified that produced stimulation of ATPase activity. A unique stimulation of BBMV ATPase activity occurred at acidic pH in the presence of 1 mM ZnCl2. In the absence of Zn2+, a second ATPase activity was stimulated by alkaline pH values with peak stimulation occurring between pH 8.5 and 9.0. The results suggest that the alkaline pH-stimulated hydrolysis of ATP probably represents the activity of BBMV alkaline phosphatase. The unique acidic pH + Zn2(+)-stimulated ATPase activity must represent the activity of a second protein other than the alkaline phosphatase, since purified alkaline phosphatase did not show this activity. The biochemical identity and physiological function of this renal BBMV ATPase activity remain to be determined, but it may be an ecto-ATPase.

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