Self-association of rabbit muscle phosphofructokinase at pH 7.0: Stoichiometry

Lyndal K. Hesterberg, James Lee

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Abstract

The self-association of rabbit muscle phosphofructokinase at pH 7.0 was investigated by velocity sedimentation. The process was demonstrated to be in a rapid, dynamic equilibrium. The concentration dependence of the weight-average sedimentation coefficient was monitored within the range of 10-750 μg/mL. The sedimentation properties of phosphofructokinase were analyzed by theoretical simulations for an associating system in rapid equilibrium. In the absence of any ligands and at a temperature of 23°C, the simplest computed model which gives the best fit between theoretical and experimental points can be described as progressive association of monomer ⇌ tetramer ⇌ 16-mer with apparent equilibrium constants K4 = 5.06 × 105 (mL/mg)3 and K16 = 3.25 × 1023 (mL/mg)15. However, at 5°C, the equilibrium was altered and can best be described as monomer ⇌ dimer ⇌ tetramer ⇌ 16-mer.

Original languageEnglish (US)
Pages (from-to)2974-2980
Number of pages7
JournalBiochemistry
Volume20
Issue number10
StatePublished - 1981
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry

Cite this

Hesterberg, L. K., & Lee, J. (1981). Self-association of rabbit muscle phosphofructokinase at pH 7.0: Stoichiometry. Biochemistry, 20(10), 2974-2980.