[Analysis of stationary kinetics of translation elongation within the framework stereospecific stabilization hypothesis of codon- anticodon complexes in a ribosome. I. Kinetic schemes of factorless elongation].

Dependences of steady-state rates of polypeptide elongation on concentrations of substrate (aminoacyl-tRNA) and product (deacylated tRNA) in the absence of elongation factors and GTP are theoretically analyzed in context of stereospecific stabilization of the codon-anticodon complexes at a ribosome. General kinetic scheme and different ribosome isomerization stages are examined. The effect of isomerization stage allows to identify reaction stage experimentally. Regulation of the direct reaction by product and regulation of the reverse reaction by substrate are possible. Under certain conditions elongation system may show kinetic cooperativity.