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cDNA clones for chalcone synthase (CHS) of Pueraria lobata cultured cells were isolated by screening the cDNA library using CHS cDNA of Phaseolus vulgaris as a probe. Analysis of nucleotide sequences of the cloned cDNA revealed a 1170-bp open reading frame that encoded a 390-amino acid polypeptide with an Mr of 43,000. The full-length cDNA was cloned into the expression vector pT7-7. CHS activity was found in the crude extracts of transformed E. coli after induction and two protein bands of ca. 43 and 34 kd were hybridized with anti-persley CHS antiserum.

Isolation, sequence and bacterial expression of a cDNA for chalcone synthase from the cultured cells of Pueraria lobata.