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SOLUBILIZATION OF PHOSPHOFRUCTOKINASE FROM THE PARTICULATE FRACTION OF CHICKEN MUSCLE
GRADY W. CHISM,
HERBERT O. HULTIN,
GRADY W. CHISM
Department of Food Science and Nutrition University of Massachusetts Amherst, Massachusetts 01002
Department of Food Science and Nutrition, The Ohio State University, Columbus, Ohio 43210
Search for more papers by this authorHERBERT O. HULTIN
Department of Food Science and Nutrition University of Massachusetts Amherst, Massachusetts 01002
Search for more papers by this authorGRADY W. CHISM,
HERBERT O. HULTIN,
GRADY W. CHISM
Department of Food Science and Nutrition University of Massachusetts Amherst, Massachusetts 01002
Department of Food Science and Nutrition, The Ohio State University, Columbus, Ohio 43210
Search for more papers by this authorHERBERT O. HULTIN
Department of Food Science and Nutrition University of Massachusetts Amherst, Massachusetts 01002
Search for more papers by this authorAbstract
The particulate fraction of chicken breast muscle (pH 6.5–6.7) contained 99% of the phosphofructokinase (PFK) activity. A dramatic shift from the particulate to the soluble form occurred at pH 7.05±0.10. ATP and MgATP were effective solubilizers of PFK at pH 6.7. ADP appeared to be converted to a solubilizer of PFK after incubation in the crude system. Cyclic AMP and AMP were not effective solubilizers at pH 6.7. The solubilization by ATP was dependent on the concentration of the nucleotide and could be prevented by lowering the pH to 6.0. Pyruvate, fructose-6-phosphate, glucose-6-phosphate, fructose-1, 6-diphosphate, glucose-1, 6-diphosphate, 2-phosphoglycerate, 2, 3-diphosphoglycerate, 3-phosphoglycerate and pyrophosphate were not effective solubilizers at pH 6.7 at the concentrations tested.
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