Lactate dehydrogenase isoenzyme pattern and total LDH activity in the lung and liver of rats chronically exposed to low and high oxygen concentrations

Life Sciences ◽  
1975 ◽  
Vol 17 (5) ◽  
pp. 761-766 ◽  
Author(s):  
Milos Chvapil
1991 ◽  
Vol 37 (10) ◽  
pp. 1805-1805
Author(s):  
A M Castaldo ◽  
G Russo ◽  
P Castaldo ◽  
R Minella ◽  
A Castaldo

1978 ◽  
Vol 170 (2) ◽  
pp. 193-201 ◽  
Author(s):  
M S Setchenska ◽  
H R V Arnstein

1. Differentiation and maturation of rabbit bone-marrow erythroid cells was accompanied by a 15-fold decrease in lactate dehydrogenase activity from approx. 0.1pmol of NADH utilized/min per cell in basophilic cells to 0.007 pmol of NADH/min per cell in reticulocytes. 2. In early cells, cell division takes place with a corresponding decrease in cell volume, but the concentration of lactate dehydrogenase remains almost constant. 3. When cell division ceases, qualitative as well as quantitative changes in the lactate dehydrogenase isoenzyme pattern become apparent and reticulocytes were found to contain almost exclusively the H4 isoenzyme, whereas early erythroblasts contained also the M4 and hybrid isoenzymes. 4. Extracts from a lysosome-enriched subcellular fraction of bone-marrow erythroid cells specifically degraded the M4 isoenzyme in vitro, but the H4 form was stable. It is suggested that lysosomal enzymes are involved in bringing about the observed changes in lactate dehydrogenase isoenzyme patterns in vivo.


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