Tou J S, Violand B N, Schlittler M R, Jennings M G
Monsanto Company, St. Louis, Missouri 63198.
J Protein Chem. 1993 Apr;12(2):237-45. doi: 10.1007/BF01026046.
Two major dimers are generated during the folding/oxidation of inclusion bodies of recombinant bovine somatotropin (bST). These dimers represent the major part of the inactive high molecular weight species that are formed in this process. The structures of the two dimers are unambiguously determined by peptide mapping using trypsin, thrombin cleavage, and selective DTT reduction experiments. Results indicate that the formation of both dimers involves the large disulfide loop cysteines. The latter-eluting dimer from RP-HPLC, previously reported as a large loop concatenated dimer, was revised to be an antiparallel disulfide-linked dimer. On the other hand, the first eluting dimer is a concatenane in which two monomers are held together by the interlocking of the two large disulfide loops.
在重组牛生长激素（bST）包涵体的折叠/氧化过程中产生了两种主要的二聚体。这些二聚体代表了在此过程中形成的无活性高分子量物种的主要部分。通过使用胰蛋白酶的肽图谱分析、凝血酶切割和选择性二硫苏糖醇（DTT）还原实验，明确确定了这两种二聚体的结构。结果表明，两种二聚体的形成都涉及到大的二硫键环半胱氨酸。反相高效液相色谱（RP-HPLC）中后洗脱的二聚体，先前报道为大环串联二聚体，现修正为反平行二硫键连接的二聚体。另一方面，先洗脱的二聚体是一种连环体，其中两个单体通过两个大二硫键环的互锁结合在一起。
