
%0 Journal Article
%A Nicholas, DJD 
%A V Deering, Judy 
%T Repression, Derepression and Activation of Nitrogenase in Azotobacter Vinelandii
%J Australian Journal of Biological Sciences
%D 1976/03/01
%V 29
%N 2
%P 147-162
%K 
%R https://doi.org/10.1071/BI9760147
%U https://www.publish.csiro.au/paper/BI9760147 
%X Ammonium ions repressed nitrogenase in cells fixing N2 gas. Immunological tests and electrophoresIs in various gels show that component I (Fe-Mo-S protein) was completely repressed by ammonium, whereas component II (Fe-S protein) apoprotein was not markedly affected. Component II from ammonium-grown cells, however, was inactive since it did not cross react with component I to reduce C2H2 to C2H4 ? The inactive component II apoprotein is immunologically identical to its active counterpart from cells fixing N2 ? Identical protein patterns were also observed in various gel-electrophoresis systems. Oxygen-inactivated component II may be reactivated with FeS04' This salt is preferable to ferrous ammonium sulphate which inactivated component I. Immunodiffusion under aerobic conditions shows that purified component I is composed of aggregated and non-aggregated forms which are antigenically distinct. The aggregate was dissociated by treatment with sodium dodecyl sulphate (SDS) into a single antigenic species which was further resolved into two subunits on SDS disc polyacrylamide gel electrophoresis. 
