I I Rapanovich

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The specific elution of rabbit skeletal muscle phosphofructokinase (PFK) from DEAE-cellulose is studied in the linear gradient of different allosteric ligands. Citrate and fructose-6-phosphate elute PFK at concentrations of 1.0 and 2.5 mM respectively, i.e. without increasing the ionic strength of the starting buffer (similar to 0.12). The specificity of(More)
The sedimentation behaviour of the subform of rabbit muscle phosphofructokinase specifically eluted from DEAE cellulose by citrate was studied in different media by velocity experiments. The measured sedimentation coefficients of different components in the system can be classified into 12 groups, which is indicative of a complex multistep association(More)
On the example of complex allosteric kinetics of phosphofructokinase from human erythrocytes we analysed the applicability of the Monod-Wyman-Changeux and association--dissociation models to the unified description of the kinetics of the oligomeric enzymes. It was shown that these models were not sufficient to construct an adequate phosphofructokinase(More)
A general statistical-thermodynamical theory of the oligomeric enzymes was applied for description of the complex regulatory properties of human erythrocyte phosphofructokinase (PFC, EC 2.7.1.11), experimental data were obtained by Wenzel et al. (Eur. J. Biochem. 1976. V. 61. P. 181). Simple two-ligand and hierarchical three-ligand models for polymeric(More)
A complex of programs in BASIC has been elaborated, the first part of which is intended for the calculation of concentrations of different ionic forms of the metabolites that are engaged in a complex equilibrium system of the metal-ligand mixture-H+ type. The second part of the complex is employed in the simulation of allosteric kinetics on the basis of the(More)
Some properties of three interconvertible forms of rabbit muscle phosphofructokinase specifically eluted from DEAE-cellulose with 19 mM citrate in 0.1 M tris-phosphate buffer, pH 8,0 (I), with 0,3 M buffer (II) and 1.5 M NaCl (III) are compared. Forms I-III differ in specific activities, alpha-helices content and sedimentation properties. The kinetic(More)
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