Fretheim K, Sleigh R W, Burley R W
Lipids. 1986 Feb;21(2):127-31. doi: 10.1007/BF02534433.
In a study of lipid-protein interactions in egg yolk, it was found that L-alpha-dipalmitoyl lecithin gave two distinct noncovalent complexes (A and B) with apovitellenin I, an apoprotein in the major yolk lipoprotein. Interaction took place under widely varied conditions, and yolk lecithin gave similar complexes. Complex A, which was formed within minutes, consisted of round particles of about 9 nm diameter. Complex B, which was formed more slowly, consisted of larger particles, possibly resembling curved discs, with diameter of 30-40 nm. The preparation and some properties of these complexes are described. It is suggested that they may be suitable for an extensive study of phospholipid-protein interactions in yolk.
在一项关于蛋黄中脂类与蛋白质相互作用的研究中，发现L-α-二棕榈酰卵磷脂与卵黄磷蛋白原I（主要蛋黄脂蛋白中的一种载脂蛋白）形成了两种不同的非共价复合物（A和B）。相互作用在广泛不同的条件下发生，并且蛋黄卵磷脂也形成了类似的复合物。复合物A在几分钟内形成，由直径约9纳米的圆形颗粒组成。复合物B形成得较慢，由较大的颗粒组成，可能类似弯曲的圆盘，直径为30 - 40纳米。描述了这些复合物的制备方法和一些性质。有人认为它们可能适用于对蛋黄中磷脂 - 蛋白质相互作用进行广泛研究。
