Rabbit muscle lactate dehydrogenase

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...

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).]... 

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).

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,... 

Tryptophan as Intermediate in Dehydrogenase Action. III. Evidence for Complete Cycle of Hydrogen Transfer between Substrate and Tryptophanyl Residues in Rabbit Muscle Lactate Dehydrogenase. J, Biol. Chem. 242, 1815-1820 (1967). 

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). 

Jervis used porous silica coated with chemisorbed polyacrylhydrazide for immobilization of adenosine monophosphate (AMP) [117]. After periodate oxidation of its ribose residue the ligand was coupled to the carrier and used for isolation of lactate dehydrogenase from rabbit muscle. The specific capacity was 2 mg of protein/g adsorbent with a ligand content of 10 pmol/g, whereas recovery of enzymatic activity after elution was 85%. Hipwell et al. [118] found that for effective binding of lactate dehydrogenases on AMP-o-aminoalkyl-Sepharose the spacer arm length required at least 4 methylene links. Apparently, a macromolecule of polyacrylhydrazide acts itself like an extended spacer arm and thus allow AMP to bind the enzyme. 

Lactate dehydrogenase Rabbit muscle Dissociation 7.0 5 -62 Schmid et al. (1979)... 

L-lactate dehydrogenase from rabbit muscle (E.C. 1.1.1.27) (25 units) methanol (analytical grade) methylene chloride (analytical grade)... 

M. Romano and M. Cerra, The action of crystalline lactate dehydrogenase from rabbit muscle on glyoxylate, Biochim. Biophys. Acta, 177, 421 26 (1969). 

Glucose oxidase (Aspergillus nigei) 4.2 Lactate dehydrogenase (rabbit muscle) 8.6... 

Lactate dehydrogenase (from rabbit muscle, EC 1.1.1.27) was purchased from Orintal Yeast Co. Raffinose and trehalose were purchased from Sigma Co. All other chemicals used in this study were reagent grade and were purchased from Wako Pure Chemical Co. Deionized distilled water was used in the experiments. 

L-Lactate dehydrogenase Origin rabbit muscle Biozyme... 

L-Lactate Dehydrogenase Origin rabbit muscle Fluka... 

Lactate dehydrogenases use several 2-hydroxy and 2 keto acids and other analogs as substrates 75-79). With the rabbit muscle enzyme (77),... 

Despite the fact that they can be much more reactive than nitrenes, carbene derivatives are less frequently cited in reports on photoaffinity labels. Two such derivatives of thyroid hormone have been described in which the amino group of the alanine side chain of 3,5,3 -triiodo-L-thyronine or 3,5,3, 5 -tetraiodo-L-thyronine was derivatized with 2-diazo-3,3,3-trifluoropropionate (246). Irradiation at 254 nm of these compounds with several cell lines yielded low incorporation of reagent (0.5-13.5%) into two forms of thyroid hormone receptor proteins. Low incorporation was also characteristic of early reports of photoaffinity labeling (e.g., 247) in which 0 -ethyl-2-diazomalonyl-cAMP and A, C)2. (ji(ethyl-2-diazomalonyl)-cAMP were used to generate carbenes which modify rabbit muscle phosphofructokinase. Similarly, only 3-14% of the potential sites of lactate dehydrogenase were labeled by the carbene derived from 3-(3//-diazirino)pyridine adenine dinucleotide (248). 

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