Muscle lactate dehydrogenase

In a subsequent study Bhambhani et al. (1997) observed significant increases in blood lactate concentrations in male and female volunteers exposed to 10 ppm hydrogen sulfide, although there was not a significant change in the activities of muscle lactate dehydrogenase, citrate synthase, or cytochrome oxidase. 

Anderson BM, Kohler ST, Young RW. 1978. Interactions of Kepone with rabbit muscle lactate dehydrogenase. J Agric Food Chem 26(l) 130-133. 

Hendrickson CM, Bowden JA. 1975. The in vitro inhibition of rabbit muscle lactate dehydrogenase by mirex and Kepone. J Agric Food Chem 23 407-409. 

V. Zewe and H. J. Eromm, Kinetic studies of rabbit muscle lactate dehydrogenase, J. Biol. Chem., 237(5), 1668-1675 (1962). 

Figure 1. Effect of lactate and pyruvate concentrations on the equilibrium exchange rates of rabbit muscle lactate dehydrogenase at pH 7.9. Reaction mixtures contained 1.68-1.70 mM NAD+, 32.2-45.5 mM NADH, and the indicated concentrations of pyruvate and lactate.

Figure 9-7 (A) Effect of glucose and glucose 6-phosphate concentrations on reaction rate of yeast hexokinase at equilibrium. Reaction mixtures contain 1-2.2 mM ATP, and 25.6 mM ADP at pH 6.5. From Fromm et al.51 (B) Effect of lactate and pyruvate concentrations on equilibrium reaction rates of rabbit muscle lactate dehydrogenase. Reaction mixtures contained 1.7 mM NAD+, and 30 - 46 pM NADH in Tris-nitrate buffer, pH 7.9, 25°C. From Silverstein and Boyer.53...

Elevated pyruvate concentration inhibits the heart muscle lactate dehydrogenase (LDH) isoenzyme but not the skeletal muscle LDH isoenzyme. 

Klyachko, O.S., Polosukhina, E.S. and Ozemyuk, N.D. (1992). Functional distinctions of muscle lactate dehydrogenase in fishes adapted to different environmental temperature (In Russian). Doklady Akademii Nauk SSSR 325,1246-1251. 

Baskakov, I., A. Wang, and D.W. Bolen (1998). Trimethylamine-N-oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function A test of the counteraction hypothesis. Biophys. J. 74 2666-2673. 

Figure 3.27 illustrates a rectangular hyperbolic plot [Equation (3.169)], doublereciprocal plot [Equation (3.170)], Scatchard plot [Equation (3.171a)], and Hames plot [Equation (3.171b)] for the binding of NADH to rabbit muscle lactate dehydrogenase. 

FIGURE 3.27 Binding of NADH with rabbit muscle lactate dehydrogenase using various methods of presenting experimental data. [Graphs reconstructed from data by Ward and Winzor, Biochem. J., 215, 685 (1983).]... 

Fig. 18. Chain trace (centre) of a subunit of dogfish muscle lactate dehydrogenase. Diagrammatic representations (corners) show constituent parts of the structure, and their relationship to the bound coenzyme. From the work of Rossmann and colleagues [79],...

It was put on the market under the name Kepone, primarily for the control of chewing insects. It acts as a stomach poison and is moderately toxic to warmblooded organisms (ld5q = 95-140 mg/kg for rats). Its mechanism of action might be based on a direct interaction with muscle lactate dehydrogenase (Anderson et al., 1978). 

Due to the high degree of molecular symmetry, it is a very stable compound, which is reflected by its extraordinarily high melting point (485°C). It is a potent paralyser of muscle lactate dehydrogenase activity (Hendrickson and Bowden,... 

Similar values were obtained for rabbit, dogfish, and bovine muscle lactate dehydrogenases (131). A wide range of values has been reported (93) and the binding is negatively cooperative (93). 

The results of stopped-flow studies of the lactate dehydrogenase reaction have proved to be more difficult to interpret than those of alcohol dehydrogenase. The dissociation velocity constants for the binary NADH compounds of the pig heart and skeletal muscle lactate dehydrogenases are much larger than that for liver alcohol dehydrogenase, and also larger than the maximum specific rates of lactate oxidation at pH 6.0-7.0 (Table VII). Some earlier step must therefore be rate-limiting. 

In muscle, lactate dehydrogenase produces lactate from pyruvate, whereas in the heart it preferentially synthesizes pyruvate from lactate. Explain how this is possible. 

The role of DIP in the thermostabilization of enzymes remains questionable. This solute was shown to have a positive effect on the stabilization of glyceraldehyde-3-phosphate dehydrogenase, but did not increase the stability of hydrogenase and pyruvate ferredoxin oxidoreductase of Thermotoga maritima or rabbit muscle lactate dehydrogenase. ... 

Fig. 3. Protecting effect of mannosylglycerate and trehalose against thermal inactivation of rabbit muscle lactate dehydrogenase. Aliquots containing the enzyme at a concentration of SO (ig ml and the solutes (final concentration 0.5 M) were incubated for 10 min at the temperatures indicated, cooled in an ice bath, and assayed immediately for residual activity. Mannosylglycerate, black bars trehalose, shaded bars no additions, open bars. Data from A. Ramos, N. D. H. Raven, R. J. Sharp, S. Bartolucci, M. Rossi, R. Cannio, J. Lebbink, J. van der Oost, W. M. de Vos, and H. Santos, Appl. Environ. Microbiol. 63,4020 (1997).

Porcine heart and muscle Lactate dehydrogenase Lactate... 

Brucine (46), the dimethoxy derivative of strychnine, has an oral LD50 in rat of 1 mg/kg. Both strychnine and brucine quench singlet oxygen, bind to glycine receptors, and inhibit muscle lactate dehydrogenase (Wink, 1993). 

All the polymeric NAD(P)+-derivatives have been checked for their cofactor activity and compatibility with enzymatic biocatalytic processes. The polymer-linked NAD(P)" -derivatives were associated with NAD(P) -dependent enzymes such as AlDH [281, 282, 291, 292], lactate dehydrogenase [286, 292], malate dehydrogenase [288, 292] and aldehyde dehydrogenase [287]. It was found that different NAD(P)+-polymers are active as cofactors towards different enzymes. For example, polyethyleneimine and polylysine bound NAD+-derivative revealed 60% and 25% activity, respectively, as compared with the native NAD+ in the presence of rabbit muscle lactate dehydrogenase, but only minute activity (ca. 2-7%) in the presence of alanine dehydrogenase from Bacillus suhtilis [281]. A comparative study of the cofactor activity with different enzymes is a subject of great interest. Even though several studies [279] attempt to predict the structural/functional relationship for the polymer-bound NAD(P)+-derivatives,... 

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