Hahn K H, Kim H
Department of Biological Science and Engineering, Korea Advanced Institute of Science and Technology, Seoul.
J Biochem. 1991 Oct;110(4):635-40. doi: 10.1093/oxfordjournals.jbchem.a123632.
Human apohemoglobin in acidic media was found to induce fusion of phosphatidylcholine/phosphatidylserine (1:1) vesicles at low protein concentration but to fragment the same vesicles to form micellar complex at high protein concentration. The fusion was demonstrated by size increase, vesicle content mixing, lipid mixing, and electron microscopy. The micellization of phospholipid vesicles was observed by light scattering, gel filtration, and electron microscopy. The hydrophobic labeling of the apohemoglobin/vesicle complex followed by CNBr cleavage of apohemoglobin showed that an N-terminal segment of the beta subunit with a molecular weight of approximately 6,000 seems to be mainly involved in the fusion process, but the whole sequences of both alpha and beta chains participate in the micellization process.
研究发现，在酸性介质中，人载脂蛋白血红蛋白在低蛋白浓度下可诱导磷脂酰胆碱/磷脂酰丝氨酸（1:1）囊泡融合，但在高蛋白浓度下会使相同的囊泡碎片化形成胶束复合物。通过尺寸增大、囊泡内容物混合、脂质混合以及电子显微镜观察证实了融合现象。通过光散射、凝胶过滤和电子显微镜观察到了磷脂囊泡的胶束化过程。对载脂蛋白血红蛋白/囊泡复合物进行疏水标记，随后用溴化氰裂解载脂蛋白血红蛋白，结果表明，分子量约为6000的β亚基N端片段似乎主要参与融合过程，但α链和β链的整个序列都参与胶束化过程。
