An allele (Pk-1 b ) from wild-caught mice that affects the activity and kinetics of erythrocyte and liver pyruvate kinase

1981 ◽  
Vol 19 (7-8) ◽  
pp. 771-781 ◽  
Author(s):  
Karen J. Moore ◽  
Grahame Bulfield
Keyword(s):  
Pyruvate Kinase ◽  
Kinetics Of

scholarly journals Characterization and Kinetics of Isoenzymes of Pyruvate Kinase from Developing Castor Bean Endosperm

1980 ◽  
Vol 65 (6) ◽  
pp. 1188-1193 ◽  
Author(s):  
Robert J. Ireland ◽  
Vincenzo De Luca ◽  
David T. Dennis
Keyword(s):  
Pyruvate Kinase ◽  
Castor Bean ◽  
Kinetics Of

scholarly journals Kinetics of a self-amplifying substrate cycle: ADP–ATP cycling assay

2000 ◽  
Vol 350 (1) ◽  
pp. 237-243 ◽  
Author(s):  
Edelmira VALERO ◽  
Ramón VARÓN ◽  
Francisco GARCÍA-CARMONA
Keyword(s):  
Lactate Dehydrogenase ◽  
Kinetic Study ◽  
Pyruvate Kinase ◽  
Adenylate Kinase ◽  
Reaction Medium ◽  
Spectrophotometric Assay ◽  
Background Signal ◽  
Cyclic System ◽  
Exponential Increase ◽  
Kinetics Of

A kinetic study of an ATP–ADP amplification cyclic system involving the enzymes adenylate kinase, pyruvate kinase and l-lactate dehydrogenase has been made. The stoichiometry of the cycle is 2:1, because two molecules of ADP are synthesized from one each of ATP and AMP, and one molecule of ADP is converted back into one of ATP at each turn of the cycle. This results in a continuous exponential increase in the concentrations of ATP and ADP in the reaction medium, according to the equations obtained. This is therefore a substrate cycle that amplifies itself, the cycling rate increasing continuously with time. The background signal of the reagent was reduced by using apyrase to degrade ATP and ADP in the reagent, permitting detection limits as low as 16pmol of ATP and/or ADP in a continuous spectrophotometric assay.

scholarly journals A kinetic study of rabbit muscle pyruvate kinase

1973 ◽  
Vol 131 (2) ◽  
pp. 223-236 ◽  
Author(s):  
S. Ainsworth ◽  
N. Macfarlane
Keyword(s):  
Reaction Mechanism ◽  
Kinetic Study ◽  
Pyruvate Kinase ◽  
Random Order ◽  
Experimental Results ◽  
Rabbit Muscle ◽  
Dead End ◽  
Inhibition Constants ◽  
Muscle Pyruvate Kinase ◽  
Kinetics Of

The paper reports a study of the kinetics of the reaction between phosphoenolpyruvate, ADP and Mg2+ catalysed by rabbit muscle pyruvate kinase. The experimental results indicate that the reaction mechanism is equilibrium random-order in type, that the substrates and products are phosphoenolpyruvate, ADP, Mg2+, pyruvate and MgATP, and that dead-end complexes, between pyruvate, ADP and Mg2+, form randomly and exist in equilibrium with themselves and other substrate complexes. Values were determined for the Michaelis, dissociation and inhibition constants of the reaction and are compared with values ascertained by previous workers.

Effects of phenylalanine and alanine on the kinetics of bovine pyruvate kinase isoenzymes

Biochemistry ◽  
1975 ◽  
Vol 14 (18) ◽  
pp. 4041-4045 ◽  
Author(s):  
Janet M. Cardenas ◽  
J. Jeffrey Strandholm ◽  
Joan M. Miller
Keyword(s):  
Pyruvate Kinase ◽  
Pyruvate Kinase Isoenzymes ◽  
Kinetics Of

On the Role of Magnesium in the Reaction of the Pyruvate Kinase from Salmonella typhimurium

1986 ◽  
Vol 41 (11-12) ◽  
pp. 1018-1022
Author(s):  
Concepcion Garcia-Olalla ◽  
Amando Garrido-Pertierra
Keyword(s):  
Salmonella Typhimurium ◽  
Pyruvate Kinase ◽  
Binding Sites ◽  
Physiological Significance ◽  
Hill Coefficient ◽  
Magnesium Concentration ◽  
Pyruvate Kinases ◽  
Kinetics Of ◽  
Binding Behaviour

Abstract The kinetics of the two purified forms of pyruvate kinase from Salmonella typhimurium LT-2 were studied in assays at pH 6.8 where the relationships between the initial velocities of the catalysed reactions and Mg2+ are non-hyperbolic. The analysis show that Mg2+ display positive homotropic interactions in their binding behaviour with Hill coefficient values of 2.5 and 1.2 for the form I and II, respectively. The binding sites of the cation to the pyruvate kinases seem to be independent to those for phosphoenolpyruvate and adenosine 5′-diphosphate; changes in the magnesium concentration might be of physiological significance in relation to a rapid regeneration of adenosine 5′-triphosphate by means of the pyruvate kinase reaction.

Kinetics of Pyruvate Kinase from Human Placenta

1977 ◽  
Vol 5 (6) ◽  
pp. 1745-1746
Author(s):  
PATRICK J. McDERMOTT ◽  
PATRICK F. FOTTRELL
Keyword(s):  
Pyruvate Kinase ◽  
Human Placenta ◽  
Kinetics Of

scholarly journals The regulatory properties of rabbit muscle pyruvate kinase. The influence of substrate concentrations

1983 ◽  
Vol 209 (2) ◽  
pp. 401-411 ◽  
Author(s):  
S Ainsworth ◽  
J Kinderlerer ◽  
R B Gregory
Keyword(s):  
Pyruvate Kinase ◽  
Exponential Model ◽  
Rabbit Muscle ◽  
Catalysed Reaction ◽  
Dead End ◽  
Influence Of Substrate ◽  
Muscle Pyruvate Kinase ◽  
Regulatory Properties ◽  
Kinetics Of ◽  
Substrate Concentrations

The kinetics of rabbit muscle pyruvate kinase were studied in assays at pH 7.4, where the relationships between the initial velocities of the catalysed reaction and the concentrations of substrates ADP, phosphoenolpyruvate and Mg2+ are non-hyperbolic. The data were used to test the applicability of the exponential model for a regulatory enzyme, which has been here extended to describe the behaviour of a three-substrate enzyme. It appears that the data can be represented by the model and as a result permit the conclusion that the substrates influence one another's binding by the same type of charge interactions that are evident in the Michaelis-Menten kinetics of the enzyme observed at pH 6.2. Evidence is also presented indicating that MgADP acts as a dead-end inhibitor of the enzyme at pH 7.4.

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