Lactate dehydrogenase, effect

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. 

AP = alkaline phosphatase ATPase = adenosine triphosphatase Cardio = cardiovascular d = day(s) Endocr = endocrine F = female Gastro = gastrointestinal Gn pig = guinea pig GOT = glutamic-oxaloacetic transaminase GPT = glutamic-pyruvic transaminase Hemato = hematological hr = hour(s) LDH = lactate dehydrogenase LOAEL = lowest-observable-adverse-effect level M = male Musc/skel = musculoskeletal NOAEL = no-observable-adverse-effect level ... 

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]...

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). 

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. 

Andres, J., Moliner, V. and Safont, V. S. Theoretical kinetic isotope effects for the hydride-transfer step in Lactate Dehydrogenase, J. Chem. Soc. Faraday Trans., 90 (1994),... 

Figure 8.2 The effect of pH on the enzyme lactate dehydrogenase (EC 1.1.1.27). The enzyme shows maximum activity at pH 7.4 (A). When stored in buffer solutions with differing pH values for 1 h before re-assaying at pH 7.4, it shows complete recovery of activity from pH values between 5 and 9 but permanent inactivation outside these limits (B).

Hepatic Effects. Enlarged liver and elevated serum levels of hepatic enzymes indicative of liver injury (lactate dehydrogenase, 2 times above normal aspartate aminotransferase, 21 times above normal alanine aminotransferase, 100 times above normal) were observed in an individual following chronic daily exposure to vapors and spills of phenol (Merliss 1972). The symptoms lessened when the... 

Hepatic Effects. Two days after a man was splashed with a phenol-water solution over his face, chest wall, hand, and both arms, serum bilirubin increased 2-fold (Horch et al. 1994). After 5 days, serum bilirubin returned to normal. An enlarged and tender liver and increased liver enzymes in the serum were reported in a case of chronic phenol poisoning (Merliss 1972). Lactate dehydrogenase was about 2-fold greater than normal, aspartate aminotransferase was about 21-fold greater than normal, and alanine aminotransferase was about 100-fold greater than normal. The man worked in a laboratory for 13.5 years where he distilled phenol several times a day. During the process, heavy odors were detectable, phenol was often spilled on his clothes, and he noted skin irritation. 

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