Polymorphism in major urinary proteins: Molecular heterogeneity in a wild mouse population
Polymorphism in major urinary proteins: Molecular heterogeneity in a wild mouse population
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DOI：
10.1023/a:1016252703836
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发表时间：
2002-07-01
影响因子：
2.3
通讯作者：
Hurst, JL
中科院分区：
文献类型：
--
作者：
Beynon, RJ;Veggerby, C;Hurst, JL
主要尿蛋白（MUPs）在小鼠的尿液中含量很高，并且在野生捕获的个体中，MUPs的具体特征差异很大。我们在地理受限的岛屿种群中进行了详细的多态性研究，通过等电聚焦和分析离子交换色谱分析了MUP的异质性。几个MUPs被纯化到足够的量，用于电喷雾电离质谱和MALDI-TOF质谱分析内多肽酶Lys-C肽图。这样的分析结果允许鉴定三个新的MUP等位基因变体。在每一种蛋白质中，变异位点都位于多肽链的一个受限片段上，突出在蛋白质表面的一个斑块上，并通过多肽主链与中央脂钙蛋白花萼相连。多态变异限制在多肽的一个片段上可能具有功能意义，无论是在配体释放的调节中，还是在尿气味标记内个性信号的交流中。
Major urinary proteins (MUPs) are present in high levels in the urine of mice, and the specific profile of MUPs varies considerably among wild-caught individuals. We have conducted a detailed study of the polymorphic variation within a geographically constrained island population, analyzing the MUP heterogeneity by isoelectric focusing and analytical ion exchange chromatography. Several MUPs were purified in sufficient quantities for analysis by electrospray ionization mass spectrometry and MALDI-TOF mass spectrometry of endopeptidase Lys-C peptide maps. The results of such analyses permitted the identification of three new MUP allelic variants. In each of these proteins, the sites of variation were located to a restricted segment of the polypeptide chain, projecting to a patch on the surface of the protein, and connected to the central lipocalin calyx through the polypeptide backbone. The restriction of the polymorphic variation to one segment of the polypeptide may be of functional significance, either in the modulation of ligand release or in communication of individuality signals within urinary scent marks.