Kinetic mechanism of Ascaris suum phosphofructokinase desensitized to allosteric modulation by diethylpyrocarbonate modification.
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Kinetic mechanism of Ascaris suum phosphofructokinase desensitized to allosteric modulation by diethylpyrocarbonate modification.
The kinetic mechanism of phosphofructokinase has been determined at pH 8 for native enzyme and pH 6.8 for an enzyme desensitized to allosteric modulation by diethylpyrocarbonate modification. In both cases, the mechanism is predominantly steady state ordered with MgATP binding first in the direction of fructose 6-phosphate (F6P) phosphorylation and rapid equilibrium random in the direction of M...
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The nucleotide sequences of the mitochondrial DNA (mtDNA) molecules of two nematodes, Caenorhabditis elegans [13,794 nucleotide pairs (ntp)], and Ascaris suum (14,284 ntp) are presented and compared. Each molecule contains the genes for two ribosomal RNAs (+rRNA and 1-rRNA), 22 transfer RNAs (tRNAs) and 12 proteins, all of which are transcribed in the same direction. The protein genes are the s...
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Ammonium ions were shown to be much more efficient than potassium ions in activating rabbit skeletal muscle phosphofructokinase (EC 2.7.1.11). Under experimental conditions simulating physiological ones (pH 7.2, and inhibitory concentrations of ATP), the apparent dissociation constant of the phosphofructokinase-NH4+ complex was 0.33 mu. This molarity was shown to lie within the physiological co...
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Ammonium ions were shown to be much more efficient than potassium ions in activating rabbit skeletal muscle phosphofructokinase (EC 2.7.1.11). Under experimental conditions simulating physiological ones (pH 7.2, and inhibitory concentrations of ATP), the apparent dissociation constant of the phosphofructokinase-NH4+ complex was 0.33 mu. This molarity was shown to lie within the physiological co...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1987
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)47906-9