Haniu M, Hsieh P, Rohde M F, Kenney W C
Department of Protein Structure, Amgen Inc., Thousand Oaks, California 91320-1789.
Arch Biochem Biophys. 1994 May 1;310(2):433-7. doi: 10.1006/abbi.1994.1189.
Intermolecular and intramolecular disulfide linkages of recombinant human platelet-derived growth factor A chain dimer were determined by chemical methods including selective reduction-alkylation, peptide isolation, or detection of diphenylthiohydantoin derivative of cystine from Edman reactions. Cys-37 and Cys-46 were selectively reduced with reducing agents under native conditions and revealed to be involved in intermolecular bridges. Other disulfide linkages including Cys-10-Cys-54, Cys-43-Cys-91, and Cys-47-Cys-93 form intramolecular bridges. The disulfide structure is homologous to that of platelet-derived growth factor B chain dimer.
重组人血小板衍生生长因子A链二聚体的分子间和分子内二硫键通过化学方法确定，包括选择性还原烷基化、肽分离或从埃德曼反应中检测胱氨酸的二苯硫代乙内酰脲衍生物。在天然条件下，用还原剂选择性还原Cys-37和Cys-46，结果表明它们参与分子间桥连。其他二硫键，包括Cys-10-Cys-54、Cys-43-Cys-91和Cys-47-Cys-93形成分子内桥连。二硫键结构与血小板衍生生长因子B链二聚体的结构同源。
