The induction of mitochondrial L-3-glycerophosphate dehydrogenase by thyroid hormone.
L-3-Glycerophosphate dehydrogenase was purified from porcine brain mitochondria by a shorter and simpler procedure than previously reported. Immunoblotting with antiserum to the porcine enzyme established that rat liver L-3-glycerophosphate dehydrogenase has the same Mr (76 000) by SDS-polyacrylamide gel electrophoresis. In liver mitochondria from normal and hyperthyroid rats, changes in L-3-glycerophosphate dehydrogenase activity were parallelled by changes in enzyme content assayed by immunoblotting. Similar changes were found in the amount of enzyme synthesised in vitro by reticulocyte lysate programmed with rat liver mRNA, suggesting that thyroid hormone causes specific induction of L-3-glycerophosphate dehydrogenase mRNA.
D000818:Animals; D001921:Brain / Q000201:enzymology; D004790:Enzyme Induction; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D005993:Glycerolphosphate Dehydrogenase / Q000096:biosynthesis*; D006980:Hyperthyroidism / Q000201:enzymology*; D007163:Immunosorbent Techniques; D008297:Male; D008930:Mitochondria, Liver / Q000201:enzymology*; D008970:Molecular Weight; D009245:NADH Dehydrogenase / Q000378:metabolism; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D013552:Swine
D012333:RNA, Messenger; D005182:Flavin-Adenine Dinucleotide; D005993:Glycerolphosphate Dehydrogenase; D009245:NADH Dehydrogenase