Schick L, Butler L G
J Cell Biol. 1969 Jul;42(1):235-40. doi: 10.1083/jcb.42.1.235.
Stimulation of Mg(2+)-dependent inorganic pyrophosphatase activity several fold by disruption of mitochondrial membranes does not appreciably alter the catalytic properties of the enzyme. Stimulation is due to increased accessibility of substrate to the enzyme, which is not solublized on activation. The enzyme is attached to the inside of the inner membrane, and under physiological conditions probably hydrolyzes only intramitochondrially-produced PP(i).
通过破坏线粒体膜使镁离子依赖性无机焦磷酸酶活性提高几倍,并不会明显改变该酶的催化特性。这种激活是由于底物与酶的接触增加,激活时酶并未溶解。该酶附着于内膜内侧,在生理条件下可能仅水解线粒体内产生的焦磷酸(PP(i))。