Keratin was extracted from rabbit hair using L-cystein as reductive agent under the condition which is pH=10.5，L-cystein 0.165 mol/L，urea 8mol/L，reaction time 5h，reaction temperature 75℃. The results of the experiments presented the dissolution rate of rabbit hair was 74.12%，the recovery rate of final keratin after disdialysis and freeze drying of dissolved solution was 69.23%，in which the mass fraction of keratin was as high as 99.38%. The molecular weight of rabbit hair keratin mainly concentrated in about 11 kDa via polyacrylamide electrophoresis SDS-PAGE.The internal structure of Keratin was characterized by infrared spectrum (FTIR)， Raman spectroscopy，X-ray diffraction (XRD) and differential scanning calorimetry (DSC). From the result，with the process of rabbit hair dissolution，about 35% (in mole fraction)disulfide bond in the rabbit hair was destoried by L-cystein，which resulted in the change of keratin secondary structure in which the content of α-helix structure decreased，and the content of β-sheet increased.