Kinetic studies of human polymorphonuclear leukocyte phosphofructokinase.
Phosphofructokinase from human polymorphonuclear leukocytes has low cooperativity and high affinity for its substrate, F-6-P. It is resistant to ATP inhibition at pH 8; however, at pH 7.1 it becomes sensitive to the effect of this compound. It is activated by F-1, 6-P2; it is not very sensitive to citrate inhibition and F-2, 6-P2 has no effect on its activity. With these kinetic characteristics we assume that perhaps the predominant L-type subunit is accompanied by an F-type component.
Campos
G
G
Instituto de Investigaciones Clínicas, Facultad de Medicina, Universidad del Zulia, Maracaibo, Venezuela.
Ryder
E
E
Morales
L M
LM
Raleigh
X
X
D002951:Citrates / Q000494:pharmacology; D004789:Enzyme Activation; D005635:Fructosediphosphates / Q000494:pharmacology; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D009504:Neutrophils / Q000201:enzymology*; D010732:Phosphofructokinase-1 / Q000037:antagonists & inhibitors / Q000097:blood*; D012016:Reference Values
D002951:Citrates; D005635:Fructosediphosphates; C027652:fructose 2,6-diphosphate; D010732:Phosphofructokinase-1; C029063:fructose-1,6-diphosphate