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 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

Pathway and kinetics of prednisolone metabolism in the human placenta

1993 ◽  
Vol 44 (3) ◽  
pp. 315-320 ◽  
Author(s):  
R.S. Addison ◽  
D.J. Maguire ◽  
R.H. Mortimer ◽  
M.S. Roberts ◽  
G.R. Cannell
Keyword(s):  
Human Placenta ◽  
Kinetics Of

The kinetics of mercury in the human placenta: Relationship between genotype and phenotype in healthy and diseased placentas

Placenta ◽  
2019 ◽  
Vol 83 ◽  
pp. e113
Author(s):  
Sebastian Granitzer ◽  
Martin Forsthuber ◽  
Raimund Widhalm ◽  
Isabella Ellinger ◽  
Harald Zeisler ◽  
...  
Keyword(s):  
Human Placenta ◽  
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.

scholarly journals KINETICS OF NICOTINAMIDE NUCLEOTIDE TRANSHYDROGENATION BY HUMAN PLACENTA

1965 ◽  
Vol 95 (1) ◽  
pp. 150-155 ◽  
Author(s):  
DD HAGERMAN ◽  
CA VILLEE
Keyword(s):  
Human Placenta ◽  
Kinetics Of

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
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