Livne A, Bar-Yaakov O
Biochim Biophys Acta. 1976 Jan 21;419(2):358-64. doi: 10.1016/0005-2736(76)90362-x.
Acetylcholinesterase activity of human erythrocytes is known to be inhibited by linolenoyl sorbitol, the inhibition being critically dependent on cell membrane intactness. The extent of enzyme inhibition by the added lipid is correlated with the magnitude of Cl- gradient across the erythrocyte membrane, indicating that enzyme sensitivity is associated with a transmembrane potential. If linolenoyl sorbitol is allowed to interact with the erythrocytes while a Cl- gradient exists, enzyme sensitivity can subsequently be demonstrated not only in the absence of a gradient but even when the cells are lyzed. It is consluded that the transmembrane potential determines the accessibility of a membrane component to the added lipid.
已知亚麻酸山梨醇可抑制人红细胞的乙酰胆碱酯酶活性，这种抑制作用严重依赖于细胞膜的完整性。添加的脂质对酶的抑制程度与红细胞膜两侧氯离子梯度的大小相关，这表明酶的敏感性与跨膜电位有关。如果在存在氯离子梯度的情况下让亚麻酸山梨醇与红细胞相互作用，随后不仅在没有梯度的情况下，甚至在细胞裂解时也能证明酶的敏感性。由此得出结论，跨膜电位决定了膜成分对添加脂质的可及性。
