Mao S Y, Maki A H, de Haas G H
FEBS Lett. 1985 Jun 3;185(1):71-5. doi: 10.1016/0014-5793(85)80743-2.
We have investigated the binding of porcine pancreatic phospholipase A2 (PA2) to n-hexadecylphosphocholine (C16PN) micelles using optical detection of triplet state magnetic resonance (ODMR) spectroscopy. The zero field splittings (zfs) of the single Trp3 residue undergo significant changes upon binding of PA2 to C16PN micelles. Zfs titrations of PA2 vs C16PN indicate that the binding stoichiometry is C16PN:PA2 approximately 25. A reduction of the (E) parameter from 1.227 to 1.135 GHz is postulated to result from Stark effects caused by the binding of a polar group (possibly phosphocholine) near Trp3 in the PA2-C16PN micelle complex.
我们利用三重态磁共振的光学检测(ODMR)光谱法研究了猪胰磷脂酶A2(PA2)与正十六烷基磷酰胆碱(C16PN)胶束的结合情况。当PA2与C16PN胶束结合时,单一色氨酸残基Trp3的零场分裂(zfs)会发生显著变化。PA2与C16PN的zfs滴定表明,结合化学计量比约为C16PN:PA2 25。(E)参数从1.227吉赫兹降至1.135吉赫兹,据推测是由于PA2-C16PN胶束复合物中靠近Trp3的一个极性基团(可能是磷酰胆碱)结合所引起的斯塔克效应导致的。