The giant salamander， as a precious amphibian， is rich in nutritional value. To fully and efficiently utilize its processing by-products， acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from giant salamander bone were isolated and characterized. The yields of salamander bone ASC and PSC were 10.71% and 13.11%， respectively. The stable triple helical structure of collagen was revealed by Fourier transform infrared spectroscopy. SDS-PAGE electropherograms showed that both samples were type I collagen with high levels of imino acids (179-187/1 000 residues). Their solubility was highest at pH 6. The thermal denaturation temperature (45.78-46.51 ℃) was significantly higher than that of marine and freshwater fish species. Under SEM， the collagen showed dense flakes and irregular holes. These results show that the characteristics of giant salamander bone collagen are similar to mammalian collagen， and it has the potential to become its substitute， which provides a basis for its subsequent research and development and utilization.