Lin H K, Holland M J, Simon E J
J Pharmacol Exp Ther. 1981 Jan;216(1):149-55.
Opiate receptor binding is inhibited by phospholipase A from some sources, whereas the enzyme from other sources is inactive even at much higher concentrations. Evidence is presented that an active enzymatic site is required for inhibition and that the degree of inhibition seems to correlate with the extent of phospholipolysis. The inhibition is reversed almost completely by treatment with 0.5 to 1% bovine serum albumin, even up to 90% inhibition by phospholipase. As more enzyme is added or incubation time is increased, the extent of reversal diminishes. Based on our evidence, the most likely explanation of these results is that the inhibition of opiate binding activity by phospholipase A is due to the toxicity of the products of phospholipolysis and that bovine serum albumin reverses the inhibition by removing these products from the membranes, thereby restoring the active conformation of the receptors.
来自某些来源的磷脂酶A可抑制阿片受体结合，而来自其他来源的该酶即使在高得多的浓度下也无活性。有证据表明，抑制作用需要一个活性酶位点，并且抑制程度似乎与磷脂分解程度相关。用0.5%至1%的牛血清白蛋白处理几乎可完全逆转这种抑制作用，即使磷脂酶的抑制率高达90%。随着添加的酶量增加或孵育时间延长，逆转程度会降低。根据我们的证据，对这些结果最可能的解释是，磷脂酶A对阿片结合活性的抑制是由于磷脂分解产物的毒性，而牛血清白蛋白通过从膜上去除这些产物来逆转抑制作用，从而恢复受体的活性构象。
