Rabbit muscle phosphofructokinase. A model for regulatory kinetic behavior.
نویسندگان
چکیده
منابع مشابه
Phosphofructokinase. III. Correlation of the regulatory kinetic and molecular properties of the rabbit muscle enzyme.
It is shown that the degree of regulatory kinetic behavior of rabbit muscle phosphofructokinase increases at a given pH and lower temperatures, as well as at a given temperature and lower pH values. It is also shown that the regulatory kinetic behavior which appears at lower pH values is inherent in the tetrameric (active) form of the enzyme. We conclude that a portion of the mechanism proposed...
متن کاملBinding of regulatory ligands to rabbit muscle phosphofructokinase. A model for nucleotide binding as a function of temperature and pH.
The binding of nucleoside triphosphates to rabbit muscle phosphofructokinase has been determined in 0.05 M phosphate buffers by changes in intrinsic protein fluorescence and by direct binding measurements. These experiments have been performed over a wide range of pH, temperature, and effector concentration. Quenching of protein fluorescence is shown to measure binding of nucleotides to a site ...
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The affinity label 5'-p-(fluorosulfonyl)benzoyl adenosine modifies rabbit muscle phosphofructokinase to the extent of one group/subunit. Modification appears to occur at a binding site specific for AMP, cyclic AMP, and ADP, i.e. those adenine nucleotides which are activators under conditions where regulatory kinetic behavior is obtained. The consequences of the modification are consistent with ...
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Chloroplast phosphofructokinase from spinach (Spinacia oleracea L.) was purified approximately 40-fold by a combination of fractionations with ammonium sulfate and acetone followed by chromatography on DEAE-Sephadex A-50. Positive cooperative kinetics was observed for the interaction between the enzyme and the substrate fructose 6-phosphate. The optimum pH shifted from 7.7 toward 7.0 as the fru...
متن کاملPurification and Some Properties of Rabbit Skeletal Muscle Phosphofructokinase.
In spite of an abundant literature (1-15) indicating that phosphofructokinasel plays a key role in the regulation of carbohydrate metabolism, few attempts have been made to purify the enzyme (4, 17, 18) since the subject of P-fructokinase was last reviewed (19). The apparent instability of the enzyme makes purification difficult, and a number of suggestions have been offered to explain this pro...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1979
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)37741-4