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.
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