Messenger RNA Coding for Phenylalanine Ammonia‐Lyase

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Abstract
The mRNA coding for phenylalanine ammonia-lyase was partially purified from irradiated cell suspension cultures of parsley (P. 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 MW of about 1.05 .times. 106 on a polyacrylamide gel. Approximately 2/3 of the polynucleotide sequence of the mRNA were estimated to be required as coding sequence for the enzyme. Phenylalanine ammonia-lyase mRNA may be unlikely to code for more than 1 of 3 coordinately induced enzymes.