Acidic and enzymatic methods were used to extract acid-soluble collagen （ASC） and enzyme-soluble collagen （PSC） from flounder bones. The UV， IR spectra， subunit composition （SDS-PAGE）， thermal stability （DSC）， microstructure（SEM） and rheological properties（DHR） of ASC and PSC were studied. UV spectra showed that ASC and PSC had the maximum UV absorption peaks at 227 nm and 226 nm， respectively. FTIR spectra showed that three helix structures of ASC and PSC were well preserved. SDS-PAGE showed that ASC and PSC were type I collagen. And heat-denatured temperature of ASC and PSC were 52.24 ℃ and 49.65 ℃ respectively； SEM showed that the cross-linked fibrous network structure was formed in ASC and PSC； DHR showed that 1% ASC or PSC solution were mainly elastic at 0.1-10 Hz oscillation frequency and had a high gel stability.