Veres L, Szabó I, Dux L
Department of Biochemistry, Albert Szent-Györgyi University Medical School, Szeged, Hungary.
Acta Biochim Biophys Hung. 1990;25(1-2):17-23.
The tryptic cleavage process of the sarcoplasmic reticulum Ca(2+)-ATPase was analysed under the influence of experimentally generated membrane potential. The digestion of the Ca2+ transport enzyme was stopped before the dissipation of the potential response. The cleavage products reflected the actual conformation of the enzyme as the low Ca2+ affinity E2, under the influence of inside positive, and as the high Ca2+ affinity E1 conformation under the influence of inside negative potential. These results provide further support for the possible role of transient membrane potential changes in the regulation of the conformational equilibrium of the sarcoplasmic reticulum Ca2+ pump enzyme.
在实验产生的膜电位影响下,分析了肌浆网Ca(2+)-ATP酶的胰蛋白酶裂解过程。在电位响应消散之前,停止了Ca2+转运酶的消化。裂解产物反映了该酶在膜内正电位影响下作为低Ca2+亲和力E2的实际构象,以及在膜内负电位影响下作为高Ca2+亲和力E1构象的实际构象。这些结果进一步支持了瞬时膜电位变化在调节肌浆网Ca2+泵酶构象平衡中可能发挥的作用。