Transcription of actin, cyclophilin and glyceraldehyde phosphate dehydrogenase genes: tissue- and treatment-specificity

Author(s):  
Gary Weisinger ◽  
Moshe Gavish ◽  
Caroline Mazurika ◽  
Oren Zinder
Development ◽  
1956 ◽  
Vol 4 (1) ◽  
pp. 93-95
Author(s):  
Richard G. Ham ◽  
Robert E. Eakin

Lallier (1954) has shown that 0·4 M lithium chloride strongly inactivates glyceraldehyde phosphate dehydrogenase—a finding which might partially explain some of the developmental changes found in lithium-treated embryos. In an attempt to establish an enzymatic basis for the morphological effects of lithium ion on Hydra which have been observed in this laboratory (Ham & Eakin, 1955), we have repeated the enzyme study with lithium chloride and extended it to include a number of other salts as controls. From typical data (Table 1), it is obvious that the inhibition of glyceraldehyde phosphate dehydrogenase activity is in no way a specific effect due to lithium ions. Both sodium chloride and potassium chloride produced a greater inhibition than did lithium chloride. From the various sodium salts tested, it was found that the anion may be of more importance than the cation in determining the degree of inhibition, although the cation also has some effect.


1986 ◽  
Vol 5 (5) ◽  
pp. 1049-1056 ◽  
Author(s):  
P.A. Michels ◽  
A. Poliszczak ◽  
K.A. Osinga ◽  
O. Misset ◽  
J. Van Beeumen ◽  
...  

1963 ◽  
Vol 41 (1) ◽  
pp. 327-333
Author(s):  
Ellen R. Gordon ◽  
D. O. Tinker ◽  
W. J. Watson

Exposure of male rats to 100% oxygen at 6 atmospheres for 20 minutes produced an increase in the concentration of fructose-1,6-diphosphate in the liver and muscle, but not in the brain. The activities of aldolase and glyceraldehyde phosphate dehydrogenase were measured in the liver and muscle. The change in the activity of these enzymes indicated that they had not become rate-limiting during exposure. The relation of these data to the Pasteur effect is considered.


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