Synthesis of rat-liver lactate dehydrogenase and characterization of its mRNA.
Rat liver lactate dehydrogenase (LDH) has been synthesized in hepatocytes and in a cell-free translation system. The subunit synthesized in both systems displayed the same electrophoretic mobility upon sodium dodecyl sulfate/polyacrylamide slab gel electrophoresis. Sequence analysis of the subunits translated in vitro and synthesized in vivo indicated N-acetyl-alanyl-alanine for both N termini. Thus, the newly synthesized subunit does not exhibit an amino-terminal extension. The mRNA for the lactate dehydrogenase subunit was exclusively found in free polysomes. A size of 2120 +/- 240 nucleotides was estimated for the mRNA. Only about 50% of these nucleotides are needed to code for the polypeptide chain of the enzyme.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002474:Cell-Free System; D002478:Cells, Cultured; D005815:Genetic Code; D007770:L-Lactate Dehydrogenase / Q000096:biosynthesis* / Q000235:genetics; D008099:Liver / Q000201:enzymology*; D008297:Male; D011061:Poly A / Q000302:isolation & purification; D011132:Polyribosomes / Q000201:enzymology; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000302:isolation & purification*; D051381:Rats; D011919:Rats, Inbred Strains
D012333:RNA, Messenger; D011061:Poly A; D007770:L-Lactate Dehydrogenase