Electrophoretic determination of fructose 6-phosphate,2-kinase.
An electrophoretic determination of fructose 6-phosphate,2-kinase activity has been devised. The enzymes partially purified from bovine liver and heart were subjected to polyacrylamide gel electrophoresis and the production of fructose 2,6-bisphosphate, coupled to the activation of potato PPi:phosphofructokinase, was detected as the dark band due to the disappearance of the fluorescence evoked by NADH consumption. The enzyme from bovine heart showed slower electrophoretic mobility than that from bovine liver, strongly suggesting the possibility that they may be distinct enzyme forms. Rat liver enzyme also gave a mobility different from that of both bovine liver and heart enzymes. Our present procedure will provide a new tool for understanding fructose-6-phosphate,2-kinase/fructose 2,6-bisphosphatase system in various tissues.
Kora-Miura
Y
Y
Third Department of Internal Medicine, Yamaguchi University School of Medicine, Japan.
Fujii
S
S
Matsuda
M
M
Sato
Y
Y
Kaku
K
K
Kaneko
T
T
D000818:Animals; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D008099:Liver / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology; D025481:Phosphofructokinase-2; D010770:Phosphotransferases / Q000032:analysis*; D011817:Rabbits; D051381:Rats
D010770:Phosphotransferases; D025481:Phosphofructokinase-2