Nakajima O, Akiyama T, Hakamatsuka T, Shibuya M, Noguchi H, Ebizuka Y, Sankawa U
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Chem Pharm Bull (Tokyo). 1991 Jul;39(7):1911-3. doi: 10.1248/cpb.39.1911.
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.
通过使用菜豆查尔酮合酶（CHS）的cDNA作为探针筛选野葛培养细胞的cDNA文库，分离出了查尔酮合酶（CHS）的cDNA克隆。对克隆的cDNA核苷酸序列分析显示，有一个1170 bp的开放阅读框，编码一个390个氨基酸的多肽，分子量为43000。将全长cDNA克隆到表达载体pT7-7中。诱导后，在转化大肠杆菌的粗提物中发现了CHS活性，并且约43 kd和34 kd的两条蛋白带与抗欧芹CHS抗血清发生杂交。
