Cyanogen bromide cleavage of proteins in sodium dodecyl sulphate/polyacrylamide gels. Diagonal peptide mapping of proteins from epidermis.
Cyanogen bromide cleavage of proteins in sodium dodecyl sulphate/polyacrylamide gels. Diagonal peptide mapping of proteins from epidermis.
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溴化氰对十二烷基硫酸钠/聚丙烯酰胺凝胶中蛋白质的裂解。
DOI：
10.1042/bj1970591
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发表时间：
1981
期刊：
影响因子：
--
通讯作者：
Dale,BA
中科院分区：
文献类型：
--
作者：
Lonsdale-Eccles,JD;Lynley,AM;Dale,BA
设计了一种采用 CNBr 的二维电泳程序来分析十二烷基硫酸钠/聚丙烯酰胺凝胶中的蛋白质。该技术可以检测一类不寻常的缺乏蛋氨酸的表皮蛋白。这些蛋白质已通过这种方法在新生小鼠、大鼠和兔子中得到鉴定，因为它们在 CNBr 存在的情况下是稳定的，因此位于对角线上。成人表皮也含有 CNBr 稳定蛋白，但含量低于新生兔子或新生啮齿动物。含蛋氨酸的蛋白质（即角蛋白）被 CNBr 降解成一系列位于对角线下方的独特和特征肽。各个角蛋白之间存在种间和种内的相似性和差异，具体取决于其蛋氨酸残基的数量和分布。啮齿动物和兔类动物蛋白质的肽图模式比人类蛋白质的肽图模式更相似。大鼠和兔子皮肤蛋白质的图谱最相似。我们得出的结论是，表皮角蛋白是一组密切相关但又各自不同的蛋白质，与一类缺乏蛋氨酸的蛋白质一起被发现。后一种蛋白质与富含组氨酸的碱性蛋白有关，这是一种与角蛋白丝聚集的表皮结构蛋白。
A two-dimensional electrophoretic procedure employing CNBr has been devised for the analysis of proteins in sodium dodecyl sulphate/polyacrylamide gels. The technique allows the detection of an unusual class of epidermal proteins that lack methionine. The proteins have been identified by this method in newborn mouse, rat, and rabbit, because they are stable in the presence of CNBr and consequently lie on a diagonal. Adult human epidermis also contains CNBr-stable proteins, but in lesser amounts than in the newborn rabbit or newborn rodents. The methionine-containing proteins (i.e., the keratins) are degraded by CNBr into a series of unique and characteristics peptides which lie below the diagonal. Inter- and intra-species similarities and differences exist between the individual keratins, depending on the number and distribution of their methionine residues. The peptide-map patterns for the rodent and lagomorph proteins are more similar to each other than to that for the human proteins. The maps for rat and rabbit skin proteins are the most similar. We conclude that the epidermal keratins are a closely related, yet individually distinct, group of proteins that are found in conjunction with a class of proteins that lack methionine. The latter proteins are related to the histidine-rich basic protein, an epidermal structural protein that aggregates with keratin filaments.