ANION-SENSITIVE ATPASE IN RABBIT CORNEAL ENDOTHELIUM AND ITS RELATION TO CORNEAL HYDRATION
ANION-SENSITIVE ATPASE IN RABBIT CORNEAL ENDOTHELIUM AND ITS RELATION TO CORNEAL HYDRATION
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DOI:
10.1016/0014-4835(77)90177-4
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发表时间:
1977-01-01
影响因子:
3.4
通讯作者:
RILEY, MV
中科院分区:
文献类型:
--
作者:
RILEY, MV
The activity of Mg2+-activated ATPase in the corneal endothelium of the rabbit is dependent on the anionic composition of the medium and is not inhibited by ouabain. Maximum anion-dependent Mg2+ ATPase activity was demonstrated in the presence of .**GRAPHIC**. followed by acetate, Cl-, .**GRAPHIC**. SCN- and OCN-. The maximum rates of ATP hydrolyzed in the presence of Mg2+, Mg2+ + .**GRAPHIC**. and Mg2+ + Na+ + K+ were 5.61 .+-. 0.7, 0.93 .+-. 0.8 and 6.74 .+-. 0.7 .mu.mol hr-1 mg-1 protein, respectively. The major part of each of these ATPase activities was found in a crude mitochondrial fraction. Activity in the presence of .**GRAPHIC**. was inhibited by 65% when 50 mM SCN- or 10 mM OCN- was added to the medium. These concentrations of inhibitor, when added to a medium perfusing intact, isolated corneas, caused a deterioration of their ability to transport fluid out of the tissue. The anion-sensitive ATPase apparently plays an important quantitative role in the energy metabolism of the endothelium, and the postulated active .**GRAPHIC**. transport across the cell layer may be influenced by this enzyme.