Selimova L M, Tashenova A A, Zaĭdes V M
Vopr Virusol. 1987 Jan-Feb;32(1):25-35.
Fractionation by polyacrylamide gel electrophoresis (PAGE) demonstrated that in the infected cells the newly synthesized influenza virus glycoproteins, hemagglutinin (HA) and neuraminidase (NA), differ from mature proteins of virus particles. After some time of life in the cells the differences are levelled. Since this phenomenon was demonstrable only in an analysis under the conditions favourable for the retention of disulphide bonds, it was designated as "disulphide maturation" of glycoproteins. Two causes of disulphide maturation of HA are considered: posttranslational folding of molecules conducive to drawing closer of the oxidizable thiol groups, and gradual loss of sensitivity to endogenous reducing agents. As for NA, the observed maturation here is the result of disulphide dimerization of monomers. Some factors affecting disulphide maturation of glycoproteins have been studied.
通过聚丙烯酰胺凝胶电泳（PAGE）进行分级分离表明，在受感染的细胞中，新合成的流感病毒糖蛋白，即血凝素（HA）和神经氨酸酶（NA），与病毒颗粒的成熟蛋白不同。在细胞中存活一段时间后，这些差异会趋于平缓。由于这种现象仅在有利于二硫键保留的条件下进行分析时才能显示出来，因此它被称为糖蛋白的“二硫键成熟”。人们认为HA二硫键成熟有两个原因：分子的翻译后折叠有利于可氧化巯基的靠近，以及对内源性还原剂敏感性的逐渐丧失。至于NA，此处观察到的成熟是单体二硫键二聚化的结果。已经研究了一些影响糖蛋白二硫键成熟的因素。
