Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
7R01GM037057-04
Application #
3291995
Study Section
Physical Biochemistry Study Section (PB)
Project Start
1989-03-01
Project End
1991-08-31
Budget Start
1989-03-01
Budget End
1989-08-31
Support Year
4
Fiscal Year
1988
Total Cost
Indirect Cost
Name
Texas College of Osteopathic Medicine
Department
Type
Schools of Osteopathy
DUNS #
City
Fort Worth
State
TX
Country
United States
Zip Code
76107
Qamar, R; Cook, P F (1993) pH dependence of the kinetic mechanism of the adenosine 3',5'-monophosphate dependent protein kinase catalytic subunit in the direction of magnesium adenosine 5'-diphosphate phosphorylation. Biochemistry 32:6802-6
McClure Jr, G D; Qamar, R; Cook, P F (1993) A method for counting active sites of cyclic AMP-dependent protein kinase. J Enzyme Inhib 7:151-7
Qamar, R; Yoon, M Y; Cook, P F (1992) Kinetic mechanism of the adenosine 3',5'-monophosphate dependent protein kinase catalytic subunit in the direction of magnesium adenosine 5'-diphosphate phosphorylation. Biochemistry 31:9986-92
Payne, M A; Cook, P F (1991) Derivation of the rate equation for competitive double activation by effectors. J Biol Chem 266:8897-8
Payne, M A; Rao, G S; Harris, B G et al. (1991) Fructose 2,6-bisphosphate and AMP increase the affinity of the Ascaris suum phosphofructokinase for fructose 6-phosphate in a process separate from the relief of ATP inhibition. J Biol Chem 266:8891-6
Rao, G S; Cook, P F; Harris, B G (1991) Effector-induced conformational transitions in Ascaris suum phosphofructokinase. A fluorescence and circular dichroism study. J Biol Chem 266:8884-90
Rao, G S; Cook, P F; Harris, B G (1991) Modification of the ATP inhibitory site of the Ascaris suum phosphofructokinase results in the stabilization of an inactive T state. Biochemistry 30:9998-10004
Kong, C T; Cook, P F (1988) Isotope partitioning in the adenosine 3',5'-monophosphate dependent protein kinase reaction indicates a steady-state random kinetic mechanism. Biochemistry 27:4795-9
Cook, P F; Rao, G S; Hofer, H W et al. (1987) Correlation between hysteresis and allosteric properties for phosphofructokinase from Ascaris suum. J Biol Chem 262:14063-7
Rao, G S; Harris, B G; Cook, P F (1987) Kinetic mechanism of Ascaris suum phosphofructokinase desensitized to allosteric modulation by diethylpyrocarbonate modification. J Biol Chem 262:14074-9

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