Isolation and characterization of apolipophorin-III from the giant water bug (Lethocerus medius).
Isolation and characterization of apolipophorin-III from the giant water bug (Lethocerus medius).
复制标题
从巨型水蝽 (Lethocerus medius) 中分离和表征载脂蛋白-III。
DOI：
10.1016/0965-1748(94)00064-o
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发表时间：
1995
影响因子：
3.8
通讯作者：
Wells,MA
中科院分区：
文献类型：
--
作者：
Kanost,MR;Sparks,KA;Wells,MA
注射合成的脂肪动力激素后，中白蛉的载脂蛋白密度降低，并与载脂蛋白-III（apoLp-III）相关。与其他apoLp-III相比，从Lethocerus medius血淋巴中分离的ApoLp-III具有Mr= 19，000和高甲硫氨酸的氨基酸组成。其圆二色性光谱与二级结构主要为α-螺旋的蛋白质一致。NH 2-末端序列与其他物种的apoLp-III序列比对显示，在每个位置，而不是特定的氨基酸残基的疏水性或亲水性的保守性。来自Lethocerus medius的ApoLp-III具有形成两亲性α-螺旋的潜力，类似于在飞蝗apoLp-III的三维结构中发现的那些。不与载脂蛋白结合的apoLp-III分子的一部分含有蓝色发色团胆绿素。
Upon injection of synthetic adipokinetic hormone, lipophorin from Lethocerus medius decreased in density and became associated with apolipophorin-III (apoLp-III). ApoLp-III isolated from hemolymph of Lethocerus medius had a Mr= 19,000 and an amino acid composition high in methionine, in comparison with other apoLp-IIIs. Its circular dichroism spectrum was consistent with a protein with secondary structure of predominantly α-helix. NH2-terminal sequence alignment with apoLp-III sequences from other species showed a conservation of the hydrophobic or hydrophilic properties of residues at each position rather than of specific amino acids. ApoLp-III from Lethocerus medius has the potential to form amphipathic α-helices, similar to those found in the three-dimensional structure of Locusta migratoria apoLp-III. A portion of the apoLp-III molecules that are not associated with lipophorin contained the blue chromophore, biliverdin.