蛋白质组学与生物信息学杂志
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大鼠脊髓可溶性和不溶性部分蛋白质的凝胶蛋白质组学表征

杨曙光、丁勤学、郭耀军、赵从健、贾玉峰、阙海平、王红霞、魏凯华、何大成、景书倩、刘少军

通过基于凝胶的蛋白质组分析仔细检查连续提取的神经可溶性和不溶性蛋白质的分级效率和蛋白质表征. Spinal cord proteins of adult rats were first extracted with aqueous buffer (fraction A), followed by standard (fraction B) or modified (fraction C) enhanced solutions. Of the top 30 most abundant proteins in fractions A, B and C, the percentage of cytoplasmic proteins was 74% (28/38) , 37% (14/38) and 42% (15/36), respectively; membrane organellar proteins accounted for 8% (3/38), 45% (17/38), and 44% (16/36); membrane proteins accounted for 13% (5/38), 18% (7/38) and 14% (5/36). The number of hydrophobic domains was 5, 15 and 9. Shared proteins in three fractions were only 13%. When additional less abundant 30 spots enriched the insoluble fraction C were characterized, membrane proteins accounted for 31%, among which 83% were peripheral membrane proteins and 17% were integral membrane proteins. Functional analysis also revealed some difference between different fractions although all fractionated proteins are involved in energy metabolism, redox regulation, signal transduction and cellular architecture.