Messenger RNA coding for phenylalanine ammonia-lyase. Characterization and partial purification from cell suspension cultures of Petroselinum hortense.
The mRNA coding for phenylalanine ammonia-lyase was partially purified from irradiated cell suspension cultures of parsley (Petroselinum hortense). The product of cell-free translation of the mRNA in a reticulocyte lysate was isolated by immunoprecipitation and compared with the native enzyme subunit. Evidence for the identity, or at least a great similarity, of both was provided by tryptic-peptide and gel-electrophoretic analyses. Under partially denaturing conditions, phenylalanine ammonia-lyase mRNA sedimented as a 20--21-S molecule in a sucrose gradient and had an apparent molecular weight of about 1.05 x 10(6) on a polyacrylamide gel. Approximately two-thirds of the polynucleotide sequence of the mRNA were estimated to be required as coding sequence for the enzyme. We suggest that phenylalanine ammonia-lyase mRNA is unlikely to code for more than of three coordinately induced enzymes.
D000642:Ammonia-Lyases / Q000096:biosynthesis*; D000818:Animals; D002478:Cells, Cultured; D007700:Kinetics; D008099:Liver / Q000378:metabolism; D010446:Peptide Fragments / Q000032:analysis; D010650:Phenylalanine Ammonia-Lyase / Q000096:biosynthesis*; D010944:Plants / Q000378:metabolism*; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000302:isolation & purification / Q000378:metabolism*; D012343:RNA, Transfer / Q000378:metabolism; D011817:Rabbits; D051381:Rats; D012156:Reticulocytes / Q000378:metabolism; D014357:Trypsin
D010446:Peptide Fragments; D012333:RNA, Messenger; D012343:RNA, Transfer; D014357:Trypsin; D000642:Ammonia-Lyases; D010650:Phenylalanine Ammonia-Lyase