Hi there
I need your help in finding a method for measuring PFK (phosphofructokinase) activity in liver.

Please help me by sending any info or references to my e-mail sbahnassy17@yahoo.com

I'm desparte for the information so please reply

sbahnassy17:

Try using the customized google life science search engine that is on Scientist Solutions. Here is a Link to the search results for 'phosphofructokinase activity in liver'


I was able to quickly find these pertinent references:

Gabaldón M, Lacomba T, Antonio. Effect of estrogens on phosphofructokinase activity of uterus, liver and kidney in rat and hamster. Steroids. 1974 Jan;23(1):105-16.



Effect of 3-deoxyglucosone on the activities of enzymes responsible for glucose metabolism in mouse liver.
Effect of 3-deoxyglucosone on the activities of enzymes responsible for glucose metabolism in mouse liver. Biol Pharm Bull. 1996 Aug;19(8):1106-8.

Abstract:
Crude extracts containing the enzymes obtained from mouse liver were incubated with 3-deoxyglucosone (3-DG), and then subjected to assay of the activities of enzymes responsible for glucose metabolism. Hexokinase and glucose-6-phosphate dehydrogenase activities were decreased by 3-DG and hexokinase activity was strongly inhibited time and concentration dependently, while glucokinase, glucose-6-phosphatase, and phosphofructokinase activities were scarcely affected. These results suggest that 3-DG inhibits the intake of glucose in the liver and a connection with development of diabetes.



UNDERWOOD AH, NEWSHOLME EA. PROPERTIES OF PHOSPHOFRUCTOKINASE FROM RAT LIVER AND THEIR RELATION TO THE CONTROL OF GLYCOLYSIS AND GLUCONEOGENESIS. Biochem J. 1965 Jun;95:868-75.

Abstract:
Phosphofructokinase from rat liver has been partially purified by ammonium sulphate precipitation so as to remove enzymes that interfere in one assay for phosphofructokinase. The properties of this enzyme were found to be similar to those of the same enzyme from other tissues (e.g. cardiac muscle, skeletal muscle and brain) that were previously investigated by other workers. 2. Low concentrations of ATP inhibited phosphofructokinase activity by decreasing the affinity of the enzyme for the other substrate, fructose 6-phosphate. Citrate, and other intermediates of the tricarboxylic acid cycle, also inhibited the activity of phosphofructokinase. 3. This inhibition was relieved by either AMP or fructose 1,6-diphosphate; however, higher concentrations of ATP decreased and finally removed the effect of these activators. 4. Ammonium sulphate protected the enzyme from inactivation, and increased the activity by relieving the inhibition due to ATP. The latter effect was similar to that of AMP. 5. Phosphofructokinase was found in the same cellular compartment as fructose 1,6-diphosphatase, namely the soluble cytoplasm. 6. The properties of phosphofructokinase and fructose 1,6-diphosphatase are compared and a theory is proposed that affords dual control of both enzymes in the liver. The relation of this to the control of glycolysis and gluconeogenesis is discussed.



Rubenchik BL, Petrun' AS. Phosphofructokinase activity and glycolysis rate in the rat liver during carcinogenesis. Biull Eksp Biol Med. 1971 Jan;71(1):68-70.
Article in Russian



Brand I, Sling HD. Kinetic properties of phosphofructokinase from rat liver and their regulatory significance for glycolysis and gluconeogenesis. Hoppe Seylers Z Physiol Chem. 1972 Oct;353(10):1505.
Article in German





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