In vitro inhibition of rabbit muscle lactate dehydrogenase by mirex and kepone

1975 ◽  
Vol 23 (3) ◽  
pp. 407-409 ◽  
Author(s):  
Constance M. Hendrickson ◽  
Joe A. Bowden
Keyword(s):  
Lactate Dehydrogenase ◽  
Rabbit Muscle ◽  
Muscle Lactate ◽  
In Vitro Inhibition

Inactivation in Vitro of Lactate Dehydrogenase-5 in Blood

1977 ◽  
Vol 14 (1-6) ◽  
pp. 48-52 ◽  
Author(s):  
A. R. Qureshi ◽  
J. H. Wilkinson
Keyword(s):  
Enzyme Activity ◽  
Lactate Dehydrogenase ◽  
Whole Blood ◽  
Rabbit Muscle ◽  
Muscle Lactate ◽  
Rabbit Blood

During incubation with rabbit blood in vitro rabbit-muscle lactate dehydrogenase-5 was inactivated at a rate similar to that observed in vivo. By contrast plasma and plasma containing erythrocytes had no effect on the enzyme activity, but plasma containing leucocytes inactivated the enzyme at the same rate as whole blood. The results obtained support the concept that intravascular inactivation accounts for the disappearance of enzymes from the circulation.

scholarly journals Kinetic Studies of Rabbit Muscle Lactate Dehydrogenase

1962 ◽  
Vol 237 (5) ◽  
pp. 1668-1675
Author(s):  
Virginia Zewe ◽  
Herbert J. Fromm
Keyword(s):  
Lactate Dehydrogenase ◽  
Kinetic Studies ◽  
Rabbit Muscle ◽  
Muscle Lactate

scholarly journals Evaluation of equilibrium constants for the interaction of lactate dehydrogenase isoenzymes with reduced nicotinamide-adenine dinucleotide by affinity chromatography

1975 ◽  
Vol 151 (3) ◽  
pp. 631-636 ◽  
Author(s):  
R I Brinkworth ◽  
C J Masters ◽  
D J Winzor
Keyword(s):  
Lactate Dehydrogenase ◽  
Affinity Chromatography ◽  
Equilibrium Constants ◽  
Mouse Tissue ◽  
Rabbit Muscle ◽  
Muscle Lactate ◽  
Sodium Phosphate Buffer ◽  
A Value ◽  
Series Of Experiments ◽  
Reduced Nicotinamide Adenine Dinucleotide

Rabbit muscle lactate dehydrogenase was subjected to frontal affinity chromatography on Sepharose-oxamate in the presence of various concentrations of NADH and sodium phosphate buffer (0.05 M, pH 6.8) containing 0.5 M-NaCl. Quantitative interpretation of the results yields an intrinsic association constant of 9.0 × 104M−1 for the interaction of enzyme with NADH at 5°C, a value that is confirmed by equilibrium-binding measurements. In a second series of experiments, zonal affinity chromatography of a mouse tissue extract under the same conditions was used to evaluate assoication constants of the order 2 × 105M−1, 3 × 105M−1, 4 × 105M−1, 7 × 105M−1 and 2 × 106M−1 for the interaction of NADH with the M4, M3H, M2H2, MH3 and H4 isoenzymes respectively of lactate dehydrogenase.

Interactions of Kepone with rabbit muscle lactate dehydrogenase

1978 ◽  
Vol 26 (1) ◽  
pp. 130-133 ◽  
Author(s):  
Bruce M. Anderson ◽  
Susan T. Kohler ◽  
Roderick W. Young
Keyword(s):  
Lactate Dehydrogenase ◽  
Rabbit Muscle ◽  
Muscle Lactate

scholarly journals Re-evaluation of the glycerol-3-phosphate dehydrogenase/l-lactate dehydrogenase enzyme system. Evidence against the direct transfer of NADH between active sites

1991 ◽  
Vol 278 (3) ◽  
pp. 875-881 ◽  
Author(s):  
S P J Brooks ◽  
K B Storey
Keyword(s):  
Lactate Dehydrogenase ◽  
Active Sites ◽  
Reaction Rate ◽  
Experimental Results ◽  
Transfer Model ◽  
Rabbit Muscle ◽  
Direct Transfer ◽  
Theoretical Predictions ◽  
Glycerol 3 Phosphate Dehydrogenase

An investigation of the direct transfer of metabolites from rabbit muscle L-lactate dehydrogenase (LDH, EC 1.1.1.27) to glycerol-3-phosphate dehydrogenase (GPDH, EC 1.1.1.8) revealed discrepancies between theoretical predictions and experimental results. Measurements of the GPDH reaction rate at a fixed NADH concentration and in the presence of increasing LDH concentrations gave experimental results similar to those previously obtained by Srivastava, Smolen, Betts, Fukushima, Spivey & Bernhard [(1989) Proc. Natl. Acad. Sci. U.S.A. 86, 6464-6468]. However, a mathematical solution of the direct-transfer-mechanism equations as described by Srivastava et al. (1989) showed that the direct-transfer model did not adequately describe the experimental behaviour of the reaction rate at increasing LDH concentrations. In addition, experiments designed to measure the formation of an LDH4.NADH.GPDH2 complex, predicted by the direct-transfer model, indicated that no significant formation of tertiary complex occurred. An examination of other kinetic models, developed to describe the LDH/GPDH/NADH system better, revealed that the experimental results may be best explained by assuming that free NADH, and not E1.NADH, is the sole substrate for GPDH. These results suggest that direct transfer of NADH between rabbit muscle LDH and GPDH does not occur in vitro.

scholarly journals The mechanism of adduct formation between NAD+ and pyruvate bound to pig heart lactate dehydrogenase

1979 ◽  
Vol 177 (3) ◽  
pp. 951-957 ◽  
Author(s):  
D C Wilton
Keyword(s):  
Lactate Dehydrogenase ◽  
Dissociation Constant ◽  
Active Site ◽  
Adduct Formation ◽  
Rabbit Muscle ◽  
Muscle Lactate

1. The rate of adduct formation between NAD+ and enol-pyruvate at the active site of lactate dehydrogenase is determined by the rate of enolization of pyruvate in solution. 2. The proportion of enol-pyruvate solutions is less than 0.01%. 3. The overall dissociation constant of adduct formation is less than 5 × 10(-8) M for pig heart lactate dehydrogenase at pH 7.0. 4. The unusual kinetics for adduct formation previously observed in the case of rabbit muscle lactate dehydrogenase [Griffin & Criddle (1970) Biochemistry 9, 1195–1205] may be attributed to the concentration of enol-pyruvate in solution being considerably less than the concentration of enzyme.

Flow kinetics of lactate dehydrogenase chemically attached to nylon tubing

1978 ◽  
Vol 56 (8) ◽  
pp. 774-779 ◽  
Author(s):  
N. J. Daka ◽  
K. J. Laidler
Keyword(s):  
Lactate Dehydrogenase ◽  
Flow Rate ◽  
Rabbit Muscle ◽  
Modified Technique ◽  
Muscle Lactate ◽  
Flow Rates ◽  
Diffusion Controlled ◽  
Michaelis Constants ◽  
Reduced Nicotinamide Adenine Dinucleotide ◽  
Nylon Tubing

Rabbit muscle lactate dehydrogenase (EC 1.1.1.27) was attached covalently to the inner surface of nylon tubing; a modified technique, involving benzidine and glutaraldehyde, was used, and the resulting immobilized enzyme showed no loss of activity over a period of several months. An experimental study was made of the flow kinetics for the reaction between pyruvate and reduced nicotinamide adenine dinucleotide in two limiting cases, one substrate in excess and the concentration of the other one varied. A range of flow rates and temperatures was covered. The results were analyzed in various ways on the basis of the Kobayashi–Laidler treatment of flow systems. It was concluded that the kinetics are largely diffusion-controlled, especially at the lower substrate concentrations and flow rates. The values of the apparent Michaelis constants vary with flow rate vf, being linear in vf−1/3, and the values extrapolated to infinite flow rate (vf−1/3 = 0) approach the values for the enzyme in free solution. Analysis of the rates led to activation energies for the diffusion of the two substrates.

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