Turnover of pegeon breast muscle pyruvate dehydrogenase complex.
The pigeon breast muscle pyruvate dehydrogenase complex was resolved into three component enzymes: lipoate acetyltransferase, pyruvate dehydrogenase, and lipoamide dehydrogenase. The antibodies against each component enzyme were prepared. All of the antibodies against component enzymes precipitated the pyruvate dehydrogenase complex. The enzyme complex was recovered as the immunoprecipitate from the extract of breast muscle of a pigeon that had received a single injection of L-[4,5-3H]leucine. The immunoprecipitate was separated into each component enzyme by SDS-polyacrylamide gel electrophoresis. The relative isotopic leucine incorporations per mg of protein into each component enzyme 4 h after the injection were 1.0 : 0.9 : 1.4 : 2.7 for lipoate acetyltransferase, alpha- and beta-subunit of pyruvate dehydrogenase, and lipoamide dehydrogenase, respectively. The half-lives of lipoate acetyltransferase, alpha- and beta-subunit of pyruvate dehydrogenase, and lipoamide dehydrogenase were 7.7, 2.5, 2.6, and 1.8 days, respectively. These results indicate that the component enzymes of the pyruvate dehydrogenase complex were synthesized and degraded at different rates.
D000818:Animals; D002950:Citrate (si)-Synthase; D010856:Columbidae; D008058:Dihydrolipoamide Dehydrogenase; D005779:Immunodiffusion; D007770:L-Lactate Dehydrogenase; D009132:Muscles / Q000201:enzymology*; D011233:Precipitin Tests; D011768:Pyruvate Dehydrogenase Complex / Q000302:isolation & purification / Q000378:metabolism*
D011768:Pyruvate Dehydrogenase Complex; D007770:L-Lactate Dehydrogenase; D008058:Dihydrolipoamide Dehydrogenase; D002950:Citrate (si)-Synthase