Crosslinked structures of the permanent set wool fiber treated with boiling water at a 40% extension state and the control fiber were studied by analyzing the rubberlike force-extension curve of the swollen fiber in a mixed solution composed of equal volumes of 8M LiBr and butyl carbitol. The thiol and disulfide contents of set fibers were also determined. It was found that (1) the disulfide (SS) bonds in low-sulfur (LS) microfibril protein transform into new crosslinkages in boiling water, but the SS bonds in high-sulfur matrix protein remain intact, (2) the SS bonds in alpha-helical segments becomes reactive only at the extension state of fiber and produces a free thiol group, and (3) intramolecular SS bonds may exist in the alpha-helical segments. Discussion was also made about the closeness of the number of crosslinkage sites of SS bonds obtained from the present rubber elasticity theory and from the theoretical analysis of the amino acid sequence of the intermediate filament. The crosslinking structure model in LS protein was proposed. It was suggested further that the setting mechanism for new crosslinkage theory seems to be unsatisfactory, since the new crosslinkages do not contribute to stabilize the extended conformation of the wool chain.