Kaplia A A, Kravtsova V V, Kravtsov A V
Biokhimiia. 1996 Jun;61(6):998-1005.
The specific sensitivity of the isoforms of the rat brain Na+,K(+)-ATPase catalytic subunit to phospholipase A2 (PL A2) from Naja naja oxiana venom has been estimated on the basis of changes in the two-component dose response curve of ouabain inhibition of Na+,K(+)-ATPase activity. Moderate Na+,K(+)-ATPase inactivation of PL A2 is accompanied by a decrease of the apparent affinity for ouabain in comparison with the untreated enzyme without any significant changes in the isoform activity ratio in the preparation. This effect is eliminated by washing of the preparation with serum albumin and seems to be mediated by the effect of free fatty acids on the enzyme. At a high level of Na+,K(+)-ATPase inactivation, the alpha-isoforms is inactivated more rapidly than the alpha (+)-isoform.
基于哇巴因抑制钠钾ATP酶活性的双组分剂量反应曲线变化,已估算出大鼠脑钠钾ATP酶催化亚基各同工型对眼镜王蛇毒磷脂酶A2(PL A2)的特异性敏感性。与未处理的酶相比,PL A2使钠钾ATP酶适度失活伴随着对哇巴因表观亲和力的降低,而制剂中同工型活性比率无任何显著变化。用血清白蛋白洗涤制剂可消除这种效应,且似乎是由游离脂肪酸对该酶的作用介导的。在钠钾ATP酶高度失活时,α-同工型比α(+)-同工型失活更快。