1972
DOI: 10.1111/j.1432-1033.1972.tb01785.x
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The Self‐Association of Rabbit‐Muscle Phosphofructokinase

Abstract: The sedimentation pattern of phosphofructokinase indicates that the enzyme undergoes a self‐association reaction. Alkaline pH and high ionic strength prevented the reaction. At pH 10.5 fructose 1, 6‐bisphosphate stabilised the “monomer” of the self‐association, which had s020,w= 11.9 ± 0.4 S, and D020,w= 3.22 ± 0.33 × 10−7 cm/sec giving a molecular weight of 340000. Sedimentation equilibrium gave a molecular weight of 330000 ± 12000. The Z‐average molecular weight, measured at pH 8 by sedimentation equilibrium… Show more

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Cited by 77 publications
(29 citation statements)
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“…Dialysis for much longer than this was impracticable since the enzyme precipitates irreversibly when dialysed exhaustively in the absence of stabilising ligands. Enzyme concentrations and specific activities were determined using an absorption coefficient a t 279 nm of 1.02 for a solution of 1 mglml [ l ] and molarities were determined using 90000 for the molecular weight of the protomer, the smallest subunit which is well characterised [23]. The ratio of absorbance a t 280 and 260nm varied between 1.6 -1.7 for different preparations.…”
Section: Methodsmentioning
confidence: 99%
“…Dialysis for much longer than this was impracticable since the enzyme precipitates irreversibly when dialysed exhaustively in the absence of stabilising ligands. Enzyme concentrations and specific activities were determined using an absorption coefficient a t 279 nm of 1.02 for a solution of 1 mglml [ l ] and molarities were determined using 90000 for the molecular weight of the protomer, the smallest subunit which is well characterised [23]. The ratio of absorbance a t 280 and 260nm varied between 1.6 -1.7 for different preparations.…”
Section: Methodsmentioning
confidence: 99%
“…The steady-state kinetic properties of the enzyme suggest it is allosteric (1) and that the catalytic activity depends on the aggregation state of the protein (2,3). The enzyme is made up of apparently identical subunits of approximately 80,000 molecular weight (4)(5)(6). Although the Stokes' radii and molecular weights of specific aggregates have been determined (2-5) and chemical crosslinking has been used to study the modes of aggregation (7), direct measurements of the size and shape of the fundamental subunit and its aggregates have not been reported.…”
mentioning
confidence: 99%
“…Enzyme species smaller than the tetramer have no appreciable enzymatic activity [la]. According to Leonard and Walker [15] the tetrameric muscle enzyme undergoes at pH 8 a closed polymerization process leading to a hexamer of this molecule with a particle weight of about two millions.…”
mentioning
confidence: 99%