Chashchin V L, Shkumatov V M, Usanov S A, Vasilevsky V I, Turko I V, Akhrem A A
Biomed Biochim Acta. 1985;44(5):665-77.
Cytochrome P-450scc consists of two domains linked with a short loop of the polypeptide chain; under its hydrolysis with trypsin the domains retain their associated state due to rigid noncovalent interactions. The structural characteristics of the individual domains have been investigated. It is established that domain I containing the haem and the adrenodoxin-binding site is the N-terminal, and domain II the C-terminal moiety of the polypeptide chain of cytochrome P-450scc.
细胞色素P - 450scc由两个通过多肽链的短环相连的结构域组成；在胰蛋白酶对其进行水解时，由于刚性的非共价相互作用，这些结构域保持其关联状态。已对各个结构域的结构特征进行了研究。现已确定，含有血红素和肾上腺皮质铁氧还蛋白结合位点的结构域I是细胞色素P - 450scc多肽链的N末端，而结构域II是其C末端部分。
