Characterization of disulfide linkages in platelet-derived growth factor AA.

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.