Shipman B A, Ryan R O, Schmidt J O, Law J H
Biochemistry. 1987 Apr 7;26(7):1885-9. doi: 10.1021/bi00381a015.
A larval-specific very high density lipoprotein (VHDL) has been isolated from the hemolymph of the honeybee Apis mellifera. VHDL was isolated by a combination of density gradient ultracentrifugation and gel filtration. The purified protein is a dimer of Mr 160,000 apoproteins as shown by chemical cross-linking with dimethyl suberimidate. N-Terminal sequence analysis indicates that the two polypeptide chains are identical. The holoprotein contains 10% lipid by weight and 2.6% covalently bound carbohydrate. A native Mr 330,000 species was obtained by gel permeation chromatography. Antiserum directed against VHDL was used to show that VHDL is distinct from other hemolymph proteins and appears to constitute a novel lipoprotein of unknown function. However, the lipoprotein is present in high amounts in hemolymph only at the end of larval life, suggesting a potential role in lipid transport and/or storage protein metabolism during metamorphosis.
已从蜜蜂意大利蜜蜂的血淋巴中分离出一种幼虫特异性的极高密度脂蛋白（VHDL）。通过密度梯度超速离心和凝胶过滤相结合的方法分离出VHDL。如用辛二亚氨酸二甲酯进行化学交联所示，纯化后的蛋白质是一种分子量为160,000的载脂蛋白二聚体。N端序列分析表明两条多肽链是相同的。全蛋白按重量计含有10%的脂质和2.6%的共价结合碳水化合物。通过凝胶渗透色谱法得到了一种天然的分子量为330,000的物质。针对VHDL的抗血清用于表明VHDL与其他血淋巴蛋白不同，似乎构成了一种功能未知的新型脂蛋白。然而，这种脂蛋白仅在幼虫期结束时在血淋巴中大量存在，这表明它在变态过程中的脂质运输和/或储存蛋白代谢中可能发挥作用。
