Molecular kinetics of beef heart lactate dehydrogenase

Biochemistry ◽  
1974 ◽  
Vol 13 (25) ◽  
pp. 5152-5158 ◽  
Author(s):  
Uwe Borgmann ◽  
Thomas W. Moon ◽  
Keith J. Laidler
Keyword(s):  
Lactate Dehydrogenase ◽  
Beef Heart ◽  
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.

Kinetics of Thyroid Hormone Induced Changes in Liver and Skeletal Muscle Enzymes of Clarias batrachus

1999 ◽  
Vol 54 (5-6) ◽  
pp. 458-462 ◽  
Author(s):  
G. Tripathi
Keyword(s):  
Skeletal Muscle ◽  
Lactate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Metabolic Enzymes ◽  
Time Dependent ◽  
Clarias Batrachus ◽  
Muscle Enzymes ◽  
Induced Changes ◽  
Kinetics Of ◽  
Mitochondrial Malate Dehydrogenase

Abstract Kinetics of triiodothyronine (T3) induced changes were studied in cytoplasmic malate dehydrogenase (cMDH), mitochondrial malate dehydrogenase (mMDH) and lactate dehydrogenase (LDH) of the liver and skeletal muscle of a catfish, Clarias batrachus. The rates of gradual inductions in the activities of all the three metabolic enzymes were faster in skeletal muscle than those of the liver. These time-dependent and tissue-specific inductions may be due to the possible differences in the rates of different enzymic syntheses. The maximum inductions in the activities of cMDH, mMDH and LDH were recorded around 19 hr after T3 treatment. Thereafter, the activities of all the enzymes gradually declined to their half levels within the next 12 hr which reflected the physiological half-life of these metabolic enzymes in the freshwater catfish.

scholarly journals Reappraisal of the Regulation of Lactococcal l-Lactate Dehydrogenase

2004 ◽  
Vol 70 (3) ◽  
pp. 1843-1846 ◽  
Author(s):  
Ed W. J. van Niel ◽  
Johan Palmfeldt ◽  
Rani Martin ◽  
Marco Paese ◽  
B�rbel Hahn-H�gerdal
Keyword(s):  
Lactate Dehydrogenase ◽  
Lactococcus Lactis ◽  
Complete Model ◽  
Substrate Level ◽  
Lactate Dehydrogenases ◽  
Kinetics Of

ABSTRACT Lactococcal lactate dehydrogenases (LDHs) are coregulated at the substrate level by at least two mechanisms: the fructose-1,6-biphosphate/phosphate ratio and the NADH/NAD ratio. Among the Lactococcus lactis species, there are strains that are predominantly regulated by the first mechanism (e.g., strain 65.1) or by the second mechanism (e.g., strain NCDO 2118). A more complete model of the kinetics of the regulation of lactococcal LDH is discussed.

scholarly journals Kinetics of activation of l-lactate dehydrogenase from Streptococcus lactis by fructose 1,6-bisphosphate

1985 ◽  
Vol 146 (1) ◽  
pp. 179-183 ◽  
Author(s):  
Michael J. HARDMAN ◽  
Vaughan L. CROW ◽  
Denise S. CRUICKSHANK ◽  
Graham G. PRITCHARD
Keyword(s):  
Lactate Dehydrogenase ◽  
Streptococcus Lactis ◽  
Fructose 1,6 Bisphosphate ◽  
Kinetics Of
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