van Loon D, Westerman J, Akeroyd R, Wirtz K W
Eur J Biochem. 1986 Jun 2;157(2):347-50. doi: 10.1111/j.1432-1033.1986.tb09675.x.
Modification by phenylisothiocyanate inhibits the phosphatidylcholine-transfer protein from bovine liver. Inhibition by this apolar reagent was greatly enhanced in the presence of vesicles, indicating that an effective modification of an essential lysine residue(s) from the interface may occur. Labeling with [14C]phenylisothiocyanate demonstrated that Lys55 was the major site of modification. We propose that Lys55 is part of the peptide segment that interacts with the membrane.
苯异硫氰酸酯的修饰会抑制来自牛肝的磷脂酰胆碱转移蛋白。在囊泡存在的情况下，这种非极性试剂的抑制作用会大大增强，这表明可能会对界面处的必需赖氨酸残基进行有效修饰。用[14C]苯异硫氰酸酯标记表明，Lys55是主要的修饰位点。我们推测Lys55是与膜相互作用的肽段的一部分。
