| D-;Rat liver and brain BDH were compared by a set of parameters, such as purification characteristics, subunit molecular weight, kinetic behavior, phospholipid activation, antibody titration, acid-urea polyacrylamide gel electrophoresis, isoelectrofocusing, and peptide mapping followed by immunochemical characterization. The enzymes are indistinguishable by these parameters. These data suggest that both tissues express the same form of the enzyme.;Relative quantification of BDH and CoA transferase were carried out using immunoblotting, in vivo synthesis and in vitro translation followed by immunoprecipitation. Activity changes of BDH found in liver and brain in developing rats were attributed to changes in the enzyme quantities, which were correlated with changes in the levels of functional BDH-mRNA in these tissues. A decrease in the activity of BDH coupled with an increase in the activity of CoA transferase in rat hepatoma cell lines resulted from changes in enzyme concentrations, which reflect the differing amounts of functional mRNA of both enzymes in these cell lines. The regulations of BDH and CoA transferase under the above conditions may be related to the adjustments of energy production or lipogenesis in these tissues and cells. |
