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SOLUBILIZATION OF PHOSPHOFRUCTOKINASE FROM THE PARTICULATE FRACTION OF CHICKEN MUSCLE
Author(s) -
CHISM GRADY W.,
HULTIN HERBERT O.
Publication year - 1977
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1977.tb00172.x
Subject(s) - phosphofructokinase , chemistry , pyrophosphate , biochemistry , fructose , solubilization , chromatography , nucleotide , glycolysis , incubation , enzyme , gene
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.