scholarly journals Effects of ifenprodil on the adenosine triphosphatase of guinea pig liver mitochondria.

1992 ◽  
Vol 100 (1) ◽  
pp. 11-20
Author(s):  
Yoshiaki YAMASHITA ◽  
Yoshimasa MIYAKE ◽  
Shigeo MITSUHIRO ◽  
Tatsuo FURUKAWA
1956 ◽  
Vol 221 (2) ◽  
pp. 697-709 ◽  
Author(s):  
Oscar Touster ◽  
V.H. Reynolds ◽  
Ruth M. Hutcheson

1982 ◽  
Vol 684 (1) ◽  
pp. 21-26 ◽  
Author(s):  
Ole Christian Ingebretsen ◽  
Per T. Normann

1982 ◽  
Vol 208 (3) ◽  
pp. 723-730 ◽  
Author(s):  
D A Shipp ◽  
M Parameswaran ◽  
I J Arinze

The capacity of foetal and neonatal liver to oxidize short-, medium- and long-chain fatty acids was studied in the guinea pig. Liver mitochondria from foetal and newborn animals were unable to synthesize ketone bodies from octanoate, but octanoylcarnitine and palmitoylcarnitine were readily ketogenic. The ketogenic capacity at 24 h after birth was as high as in adult animals. Hepatocytes isolated from term animals were unable to oxidize fatty acids, but at 6 h after birth production of 14CO2, acid-soluble products and acetoacetate from 1-14C-labelled fatty acids was 40-50% of the rates at 24 h. At 12 h of age these rates had already reached the 24 h values and did not change during suckling in the first week of life. The activities of hepatic fatty acyl-CoA synthetases, which were minimal in the foetus or at term, increased to maximal values in 12-24 h. The data show that the capacity for beta-oxidation and ketogenesis develops maximally in this species during the first 6-12 h after birth, and appears to be partly dependent on the development of fatty acid-activating enzyme.


1972 ◽  
Vol 139 (4) ◽  
pp. 1252-1257
Author(s):  
L. Garthoff ◽  
R. B. Tobin ◽  
M. A. Mehlman ◽  
V. DeVore

1984 ◽  
Vol 221 (1) ◽  
pp. 105-111 ◽  
Author(s):  
S Wicheanvonagoon ◽  
I J Arinze

Phosphoenolpyruvate carboxykinase was purified from mitochondria of guinea-pig liver by affinity chromatography on GMP-Sepharose. The enzyme was purified 100-fold to a high degree of electrophoretic homogeneity as judged by detection of a single protein band on sodium dodecyl sulphate/polyacrylamide gels. The yield was about 16%. The Mr of the purified enzyme was estimated to be 68500 +/- 680 by analysis on sodium dodecyl sulphate/polyacrylamide gels. Antibodies raised in rabbits against the purified enzyme were highly specific for mitochondrial phosphoenolpyruvate carboxykinase and did not precipitate the cytosolic form of this enzyme from either rat or guinea-pig liver cytosol. The use of this antibody showed that starvation does not increase the amount of the enzyme. However, neonatal-development-dependent increase in its activity is shown to be mediated by accumulation of phosphoenol pyruvate carboxykinase-specific protein.


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