Synthesis of the nitrogen-fixing enzyme system in oligonitrophilic bacteria

Oligonitrophilic bacteria were cultivated on a medium containing only 2.5--10.0 mg/litre of nitrogen compounds. They assimilated elementary nitrogen only after utilization of these nitrogen compounds during growth and formation of nitrogen-fixing enzyme system. Their cells grown on a medium containing high concentrations of bound nitrogen did not fix nitrogen during further incubation in the atmosphere of 15N; therefore, the enzymes involved in nitrogen fixation were induced. These organisms are characterized by diauxia during their growth on media containing "start" doses of nitrogen. Enzymes catalysing nitrogen fixation in azotobacter are also induced. But, contrary to oligonitrophilic bacteria, the azotobacter does not require nitrogen compounds in the medium in order to adapt to molecular nitrogen, and its growth curve is not of a biphasal character. These data and the evidence of other authors suggest that all nitrogen-fixing microorganisms are characterized by the induced, not constitutive, enzymes involved in reduction of molecular nitrogen.     

Physico-chemical properties of a protein-inhibitor of serine proteinases from the potato]

Serine proteases inhibitor with pl-7.3, isolated from potatoe tubers by isoelectric focusing procedure as described previously (V.V. Mosolov et al., Bioorganic Chem., 1, 1449, 1975), was homogeneous under ultracentrifugation, having sedimentation coefficient S20,w 2.8S. Its molecular weight, investigated by sedimentation equilibrium and gel filtration through Sephadex G-100, was found to be 32500 and 31500 respectively. The Stokes radius R and frictional ratio f/fo were found to be 24 A and 1.14. The molecular weight of the inhibitor as determined by sodium dodecylsulfate polyacrylamide electrophoresis was twice as low as determined in ultracentrifuge and by gel filtration procedure. It is suggested that the inhibitor is dimer and consists of two protomers of equal molecular weight.