Berrez J M, Pattus F, Latruffe N
Arch Biochem Biophys. 1985 Nov 15;243(1):62-9. doi: 10.1016/0003-9861(85)90773-8.
The strong interaction of D-beta-hydroxybutyrate dehydrogenase with phospholipid monomolecular films is demonstrated by the surface pressure increase of a film compressed up to 33 mN/m. Although the D-beta-hydroxybutyrate apodehydrogenase was able to penetrate many phospholipid monolayers, it interacted preferentially with negatively charged monolayers such as those made from diphosphatidylglycerol. The weakest interaction was found with phosphatidylcholine, which is the reactivating phospholipid for the enzyme. These interactions were dependent on the phospholipid chain length, ionic strength, and pH. At basic pH the apoenzyme lost its specificity for negatively charged phospholipids, suggesting the deprotonation of a cationic amino acid residue of the enzyme polypeptide chain. The charge effects are in agreement with results obtained using phospholipid vesicles. Beside the electrostatic interactions, the influence of phospholipid chain length and the ionic strength indicate that D-beta-hydroxybutyrate apodehydrogenase penetrates into the hydrophobic part of the lipid interface.
高达33 mN/m压缩的薄膜表面压力增加，证明了D-β-羟基丁酸脱氢酶与磷脂单分子膜的强相互作用。尽管D-β-羟基丁酸脱辅基脱氢酶能够穿透许多磷脂单层，但它优先与带负电荷的单层相互作用，如由二磷脂酰甘油制成的单层。发现与磷脂酰胆碱的相互作用最弱，而磷脂酰胆碱是该酶的再活化磷脂。这些相互作用取决于磷脂链长度、离子强度和pH值。在碱性pH值下，脱辅基酶失去了对带负电荷磷脂的特异性，表明酶多肽链上的阳离子氨基酸残基发生了去质子化。电荷效应与使用磷脂囊泡获得的结果一致。除了静电相互作用外，磷脂链长度和离子强度的影响表明，D-β-羟基丁酸脱辅基脱氢酶渗透到脂质界面的疏水部分。
