1991 Volume 39 Issue 7 Pages 1911-1913
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.