Mathew P A, Kagawa N, Bhasker C R, Waterman M R
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235.
Protein Seq Data Anal. 1990 Sep;3(4):323-5.
The primary structure of the carboxy terminal 296 amino acids of chicken cholesterol side chain cleavage cytochrome P450 (P450scc) was deduced from a partial cDNA clone isolated from a chicken ovarian cDNA library. The sequence contained putative steroid binding and heme binding regions. Comparison of this sequence with the corresponding sequences of three mammalian forms of P450scc shows greater than 50% homology. The heme binding region of the avian P450scc shows 76% homology with the heme binding regions of rat and human P450scc and 81% homology with that of bovine P450scc.
从鸡卵巢cDNA文库中分离得到的一个部分cDNA克隆推导了鸡胆固醇侧链裂解细胞色素P450（P450scc）羧基末端296个氨基酸的一级结构。该序列包含推定的类固醇结合和血红素结合区域。将此序列与三种哺乳动物形式的P450scc的相应序列进行比较，显示出超过50%的同源性。禽类P450scc的血红素结合区域与大鼠和人P450scc的血红素结合区域显示出76%的同源性，与牛P450scc的血红素结合区域显示出81%的同源性。
