LIPID DOMAINS IN THE YOLK LIPOPROTEIN COMPLEX *
LIPID DOMAINS IN THE YOLK LIPOPROTEIN COMPLEX *
复制标题
蛋黄脂蛋白复合物中的脂质结构域 *
DOI:
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发表时间:
1980
影响因子:
5.2
通讯作者:
L. Banaszak
中科院分区:
文献类型:
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作者:
Joe Ross;R. Wrenn;D. Ohlendorf;L. Banaszak
Because of the size and complexity of the serum lipoproteins, a variety of “model” lipid-protein systems have been studied with the goal of understanding their organization. One such model system is the yolk lipoprotein complex found in oocytes from oviparous animals. This yolk system in amphibian eggs is present in microcrystalline form,’ and hence can be studied by diffraction methods. To the extent that similarities exist in the overall assembly of lipid and protein between the yolk, serum, and other soluble lipoproteins, simple ordered model systems can propide a wealth of structural data. The yolk system from Xenopus laevis and other amphibia, birds, and insects contains two major components : a lipoprotein called lipovitellin and a phosphoprotein named phosvitin. This complex is derived from a precursor protein called lipovitellogenin, produced in the liver. Lipovitellogenin is transported in the serum in a form that is thought to contain two copies of a single polypeptide chain having a molecular weight in the range of 180,000-200,000.2~ This single chain polypeptide precursor is believed to be cleaved during uptake by the ovaries into phosvitin and the three different polypeptides in lipovitellin. Biochemical analysis of the yolk lipoprotein from Xenopus, combined with earlier estimates of its size, showed that it is a dimeric complex of MW 456,000.4 Each monomeric unit contains four different polypeptide chains called LV-A (MW 105,000), LV-B (MW 35,500), and LV-C (MW 32,000).4 Phosvitin, the other protein component, was found to have a molecular weight of 17,000.4 The complex contains about 17% lipid, which, by further analysis, is equivalent to a stoichiometry of about 35 molecules of phospholipid and 15 molecules of neutral lipid in each subunit of lip~vitellin.~