Berrez J M, Latruffe N, Gaudemer Y
Biochimie. 1984 Nov-Dec;66(11-12):717-22. doi: 10.1016/0300-9084(84)90261-x.
Attempts to reactivate purified D-beta-hydroxybutyrate apodehydrogenase, a lecithin-requiring enzyme, have been carried out using neutral, anionic, cationic and zwitterionic surfactants. Cationic and zwitterionic compounds exclusively are able to partially replace phosphatidylcholine, the reactivating phospholipid. The extent of reactivation depends on the steric hindrance of the polar head and on the hydrophobic tail length. A molecule bearing a positive charge and an aliphatic chain is the sole structure absolutely required for activity. However the presence of a negative charge is important for enzyme binding to amphiphilic structures and for the efficiency of reactivation.
人们尝试使用中性、阴离子、阳离子和两性离子表面活性剂来重新激活纯化的D-β-羟基丁酸脱氢酶（一种需要卵磷脂的酶）。只有阳离子和两性离子化合物能够部分替代具有重新激活作用的磷脂——磷脂酰胆碱。重新激活的程度取决于极性头部的空间位阻和疏水尾部的长度。带有正电荷和脂肪链的分子是酶活性绝对必需的唯一结构。然而，负电荷的存在对于酶与两亲结构的结合以及重新激活的效率很重要。
