Carr L G, Skatrud P L, Scheetz M E, Queener S W, Ingolia T D
Gene. 1986;48(2-3):257-66. doi: 10.1016/0378-1119(86)90084-3.
The isopenicillin N synthetase (IPS) gene from Penicillium chrysogenum was isolated from a recombinant bacteriophage lambda library using the Cephalosporium acremonium IPS (cIPS) gene as a heterologous hybridization probe. The protein coding region of the P. chrysogenum IPS (pIPS) gene was about 74% homologous to the cIPS gene, and the predicted amino acid sequences of the encoded proteins were about 73% homologous. Escherichia coli cells with the pIPS gene contained IPS activity whereas untransformed cells were completely devoid of this enzymatic activity. The transformed cells were also shown to contain an abundant protein accounting for about 10% of total cell protein which reacted strongly with anti-cIPS antiserum.
利用顶头孢霉的异青霉素N合成酶（cIPS）基因作为异源杂交探针，从重组λ噬菌体文库中分离出了产黄青霉的异青霉素N合成酶（IPS）基因。产黄青霉IPS（pIPS）基因的蛋白质编码区与cIPS基因约有74%的同源性，所编码蛋白质的预测氨基酸序列约有73%的同源性。含有pIPS基因的大肠杆菌细胞具有IPS活性，而未转化的细胞则完全没有这种酶活性。转化后的细胞还显示含有一种丰富的蛋白质，约占细胞总蛋白的10%，它与抗cIPS抗血清反应强烈。
