Enzymes of Glycerol Metabolism in Developing Rat Liver and Kidney

Enzyme ◽  
1974 ◽  
Vol 17 (3) ◽  
pp. 168-178 ◽  
Author(s):  
Helen B. Burch ◽  
Oliver H. Lowry ◽  
Lucile M. Delaney
Keyword(s):  
Rat Liver ◽  
Glycerol Metabolism ◽  
Liver And Kidney ◽  
Developing Rat

scholarly journals Arylamidases of Rat Liver and Kidney

1967 ◽  
Vol 242 (10) ◽  
pp. 2369-2374
Author(s):  
S. Mahadevan ◽  
A.L. Tappel
Keyword(s):  
Rat Liver ◽  
Liver And Kidney

scholarly journals Sialidase of Rat Liver and Kidney

1967 ◽  
Vol 242 (19) ◽  
pp. 4409-4413
Author(s):  
S. Mahadevan ◽  
J.C. Nduaguba ◽  
A.L. Tappel
Keyword(s):  
Rat Liver ◽  
Liver And Kidney

Adaptation of rat liver and kidney antioxidant defenses after d-Amphetamine repeated administration

1998 ◽  
Vol 95 ◽  
pp. 55 ◽  
Author(s):  
Félix Carvalho ◽  
Eduarda Fernandes ◽  
Fernando Remiño ◽  
Paulo Sousa ◽  
Maria de Lourdes Bastos
Keyword(s):  
Rat Liver ◽  
Repeated Administration ◽  
Antioxidant Defenses ◽  
Liver And Kidney

scholarly journals Properties of subunits of the multicatalytic proteinase complex revealed by the use of subunit-specific antibodies

1991 ◽  
Vol 278 (1) ◽  
pp. 171-177 ◽  
Author(s):  
A J Rivett ◽  
S T Sweeney
Keyword(s):  
Molecular Mass ◽  
Rat Liver ◽  
Gel Filtration ◽  
Immunoblot Analysis ◽  
Rat Tissues ◽  
Specific Antibodies ◽  
Multicatalytic Proteinase ◽  
Cell Extracts ◽  
Liver And Kidney ◽  
Lysosomal Proteinase

The multicatalytic proteinase (MCP) is a high-molecular-mass non-lysosomal proteinase that gives rise to a characteristic pattern of bands of molecular mass 22-34 kDa on SDS/PAGE gels. Isoelectric-focusing gels of the enzyme purified from rat liver show 16 bands with isoelectric points in the range of pH 5-8.5. Two-dimensional PAGE gels reveal that there are more than the previously reported 13 polypeptides associated with the MCP from rat liver and show a pattern of 15-20 major spots and several minor ones, similar to that of MCP isolated from some other sources. Possible relationships between the different polypeptides were investigated by immunoblot analysis of electrophoretically purified proteinase subunits with affinity-purified subunit-specific antibodies as well as antibodies raised against individual denatured subunits of the complex. The results demonstrate that many of the major polypeptide components of the MCP complex are antigenically distinct. Moreover comparison of immunoreactive material in crude cell extracts with that in purified MCP preparations has shown that the polypeptides are not derived from a smaller number of higher-molecular-mass subunits. Also, individual subunits have the same apparent molecular mass in a variety of rat tissues, suggesting close similarity between MCPs of different tissues. The highest concentrations of MCP subunits occur in liver and kidney. Gel-filtration analysis of crude extracts has demonstrated that MCP polypeptides are also associated with a higher-molecular-mass complex, which may be the 26 S proteinase that has been implicated in the degradation of ubiquitin-protein conjugates.

Effect of Dexamethasone on Triiodothyronine Production in the Perfused Rat Liver and Kidney*

Endocrinology ◽  
1984 ◽  
Vol 114 (1) ◽  
pp. 31-36 ◽  
Author(s):  
ANTHONY S. JENNINGS ◽  
DUNCAN C. FERGUSON
Keyword(s):  
Rat Liver ◽  
Perfused Rat Liver ◽  
Liver And Kidney

scholarly journals Induction of carnitine acetyltransferase by clofibrate in rat liver

1981 ◽  
Vol 194 (1) ◽  
pp. 249-255 ◽  
Author(s):  
B Mittal ◽  
C K R Kurup
Keyword(s):  
Protein Synthesis ◽  
Enzyme Activity ◽  
Rat Liver ◽  
Time Lag ◽  
Mitochondrial Protein ◽  
Carnitine Acetyltransferase ◽  
Enzyme Protein ◽  
General Protein Synthesis ◽  
Liver And Kidney ◽  
General Protein

Administration of the anti-hypercholesterolaemic drug clofibrate to the rat increases the activity of carnitine acetyltransferase (acetyl-CoA-carnitine O-acetyltransferase, EC 2.3.1.7) in liver and kidney. The drug-mediated increase in enzyme activity in hepatic mitochondria shows a time lag during which the activity increases in the microsomal and peroxisomal fractions. The enzyme induced in the particulate fractions is identical with one normally present in mitochondria. The increase in enzyme activity is prevented by inhibitors of RNA and general protein synthesis. Mitochondrial protein-synthetic machinery does not appear to be involved in the process. Immunoprecipitation shows increased concentration of the enzyme protein in hepatic mitochondria isolated from drug-treated animals. In these animals, the rate of synthesis of the enzyme is increased 7-fold.

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