Abstract: Phenylalanine ammonia-lyase (PAL) plays an important role in the phenylpropanoid metabolic pathway in higher plants and is closely related to the synthesis of major secondary metabolites. Ferulic acid,a major active ingredient in Angelica sinensis,is one of the intermediate products in phenylpropanoid pathway. In this paper,the cDNA fragment of phenylalanine ammonia-lyase gene (PAL) was cloned and its tissue-specific expression by fluorescence quantitative PCR was analyzed for exploring the mechanism of biosynthesis and accumulation of ferulic acid in Angelica sinensis. A pair of amplification primers was designed according to the conservative sequences of the cloned PAL. Extracting the total RNA from the leaf tissue of A. sinensis as a template,PAL fragments were obtained by reverse transcription polymerase chain reaction (RT-PCR) and connected to pGEM-T Easy vector then transformed into Escherichia coli DH5α. The positive clone identified by PCR was sequenced and 706 bp sequence (accession number: KJ000258) including termination codon TAA was obtained,which encoding 232 amino acids. The sequence identity analysis suggested that both the nucleotide sequence and its corresponding amino acid sequence shared over 80% of homology with GenBank PALs from Glehnia littoralis and five other higher plant species. Taking actin of A. sinensis as a reference gene,SYBR green fluorescence quantitative RT-PCR was used to detect the relative expression levels of PAL in leaf,stem and root of A. sinensis. The findings were PAL expressed at the highest level in leaf,followed by stem and root,and the relative expression levels in leaf and stem was 7.5 and 2.7 times relative to root,respectively.