Brunner J
Department of Biochemistry, Swiss Federal Institute of Technology ETH, Zürich, Switzerland.
FEBS Lett. 1989 Nov 6;257(2):369-72. doi: 10.1016/0014-5793(89)81574-1.
Low pH-induced binding of the bromelain-solubilized form of influenza virus hemagglutinin (BHA) to membranes occurs through the fusion peptide. From asymmetric hydrophobic photolabeling of membranes, evidence was obtained that this peptide penetrates only one leaflet of the bilayer. The asymmetrical labeling was achieved by employing a photoreactive analogue of a fatty acid whose transbilayer distribution can be manipulated by a membrane proton gradient.
低pH诱导的菠萝蛋白酶溶解形式的流感病毒血凝素（BHA）与膜的结合是通过融合肽实现的。通过对膜进行不对称疏水光标记，获得的证据表明该肽仅穿透双层膜的一个小叶。不对称标记是通过使用一种脂肪酸的光反应类似物来实现的，其跨双层分布可由膜质子梯度控制。
