Kinetic analysis of cooperativity of phosphorylated L-type pyruvate kinase

2006 ◽  
Vol 55 (4) ◽  
pp. 179
Author(s):  
I Faustova ◽  
J Järv
1975 ◽  
Vol 3 (2) ◽  
pp. 312-314 ◽  
Author(s):  
IAN G. GILES ◽  
PETER C. POAT ◽  
KENNETH A. MUNDAY

1982 ◽  
Vol 2 (10) ◽  
pp. 825-833 ◽  
Author(s):  
T. Norman Palmer ◽  
Bhanu R. Odedra

The allosteric inhibition of Ml-type pyruvate kinase from rabbit skeletal muscle by phenylalanine is reciprocally dependent on Mg2+ and phosphoenolpyruvate concentrations. At pH 8, phenylalanine acts as a competitive inhibitor with respect to Mg2+ and phosphoenolpyruvate, and vice versa. Phenylalanine introduces sigmoidicity into the dependence of the reaction velocity on [Mg2+]. In vitro kinetic analysis indicates that phenylalanine inhibition of muscle pyruvate kinase is unlikely to have regulatory significance in vivo.


1981 ◽  
Vol 110 (2) ◽  
pp. 420-423
Author(s):  
Rebecca L. Cochran ◽  
John A. Black

1970 ◽  
Vol 24 (03/04) ◽  
pp. 432-437 ◽  
Author(s):  
S Cronberg ◽  
J. P Caen

SummaryReports on platelet aggregation after addition of calcium or magnesium to EDTA- PRP or platelet suspensions were confirmed. An aggregating principle was found in the EDTA-plasma and the supernatant of the platelet suspensions. Aggregation by magnesium in a platelet suspension was inhibited by adenosine and phosphoenol- pyruvic acid and pyruvate kinase, which suggested that the active principle was identical with ADP. Degradation of ADP in EDTA plasma was blocked.It thus appears that aggregation induced by calcium or magnesium in EDTA-PRP and platelet suspension was due to accumulation of spontaneously liberated ADP, which was not degraded.


1965 ◽  
Vol 13 (01) ◽  
pp. 155-175 ◽  
Author(s):  
H. C Hemker ◽  
P.W Hemker ◽  
E. A Loeliger

SummaryApplication of the methods of enzyme-kinetic analysis to the results of clotting tests is feasible and can yield useful results. However, the standard methods of enzyme kinetics are not applicable without modifications imposed by the peculiarities of the blood-clotting enzyme system. The influence of the following complicating circumstances is calculated :1. Substrate is not present in excess.2. Only relative measures exist for concentrations of substrate or enzymes.3. Enzymes and substrates are often added together.4. Reagents are not pure.5. Clotting-time is our only measure for clotting-velocity.Formulas are deduced, which makes it possible to recognize the effect of these complications.


Sign in / Sign up

Export Citation Format

Share Document