Lactate dehydrogenase, LDH

The shift in pattern of protein synthesis during anaerobiosis has been observed in root tissue of many other plant species including rice, sorghum, barley, pea, and carrot (see Sachs Ho, 1986). In anaerobically treated barley aleurone cells, lactate dehydrogenase (LDH) activity increases (Hanson Jacobsen, 1984) as does enzyme activity and mRNA levels for ADH (Hanson, Jacobsen Zwar, 1984). 

Fig. 27. The effects of shear on the inactivation rate of lactate dehydrogenase (LDH) at different conditions. LDH are subjected to shear at a mean velocity gradient of 6490 s at 30 °C [107]...

Figure 7-11. Normal and pathologic patterns of lactate dehydrogenase (LDH) isozymes in human serum. LDH isozymes of serum were separated by electrophoresis and visualized using the coupled reaction scheme shown on the left. (NBT, nitroblue tetrazolium PMS, phenazine methylsulfate). At right is shown the stained electropherogram. Pattern A is serum from a patient with a myocardial infarct B is normal serum and C is serum from a patient with liver disease. Arabic numerals denote specific LDH isozymes.

Lactate dehydrogenase (LDH) is a nonspecific marker of hepa-tocyte damage disproportionate elevation of LDH indicates ischemic injury. 

Other possible laboratory abnormalities include elevated white blood cell count, hyperglycemia, hypocalcemia, hyperbilirubinemia, elevated serum lactate dehydrogenase (LDH), and hypertriglyceridemia. 

Laboratory tests Complete blood count, lactate dehydrogenase (LDH), renal function, and liver function tests... 

A baseline chest x-ray, lactate dehydrogenase (LDH) level, and computed tomographic (CT) scan of the chest, abdomen, and pelvis may be ordered by the oncologist as indicated clinically, depending on the patient s symptoms, the presence of lymph... 

White blood cell count greater than 50 x 103/pL (50 x 109/L) Lactate dehydrogenase (LDH) levels greater than 1500 IU/L (1500 U/L or 25 uKat/L)... 

Liver function, including AST, ALT, alkaline phosphatase, lactate dehydrogenase (LDH), total and conjugated bilirubin a comprehensive metabolic panel can be ordered (i.e., sodium, potassium, chloride, bicarbonate, blood urea nitrogen, creatinine, glucose, calcium, AST, ALT, alkaline phosphatase, albumin, and total bilirubin), but phosphorus, magnesium, and fractionated... 

K. Izutsu, S. Yoshioka, and S. Kojima, Increased stabilizating effects of amphiphilic excipients on freeze drying of lactate dehydrogenase (LDH) by dispersion into sugar matrices, Pharm. Res., 12, 838 (1995). 

Lactate dehydrogenase (LDH) LDH released by cells with damaged membrane results in the conversion of a tetrazolium compound into a water-soluble fluorescent formazan dye Cell membrane Yes [32]... 

Simon et al. [92] investigated a biocatalytic anode based on lactate oxidation by lactate dehydrogenase (LDH). The anodic current is generated by the oxidation of NADH (produced by NAD+ and substrate) while LDH catalyzes the electro-oxidation of lactate into pyruvate. As previously mentioned, the oxidation of NADH at bare electrodes requires a large overpotential, so these authors used poly(aniline) films doped with polyanions to catalyze NADH oxidation. Subsequent research by this group focused on targeting mutants of LDH that are amenable to immobilization on the polyaniline surface [93],... 

Suaud-Chagny and Gonon [3] presented a new procedure for protein immobilization adapted to carbon microelectrode characteristics. The principle of this method of immobilization is based on the association of the protein with an inert porous film immobilized around the active tip of the electrode. For this purpose the carbon was coated with an inert, electrochemically obtained protein sheath (bovine serum albumin, BSA) a few micrometers thick. Then the sheath around the fiber was impregnated with lactate dehydrogenase (LDH), which could be immobilized onto the electrode and resulted in an electrode sensitive to pyruvate. 

Figure 5. Pulmonary inflammatory response to chronic diesel exhaust exposure as measured in bronchoalveolar lavage fluid. The total amount or activity of material removed from the lung has been normalized to the weight of control lungs. Inflammatory response is indicated by influx of neutrophils (PMN). Cytotoxicity is indicated by extracellular lactate dehydrogenase (LDH). (Continued on next page.)...

Sutton [1.15] studied the question of how quickly solutions with certain CPAs (GL, dimethylsulfoxide (DMSO) and others] have to be cooled in order to avoid crystallization. At 100 °C/min concentration of 42.1 % DMSO and 48.5 % for GL are necessary to achieve the glass phase. With a 32.5 % solution of (2R.3R)-(-)butan-2,3-dio, the same effect can be accomplished at = 50 °C/min. In Fig. 1.18 Sutton (Fig. 11 from [1.114]) showed, that polyethylene glycol with a molecular weight of 400 (PEG 400) reduced the critical cooling rate down to approx. 25 °C/min. The addition of PEG 8000 [1.115] improved the protection of lactate dehydrogenase (LDH) by maltodextrins, if maltodextrins with low dextrose equivalents are used. 

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