Abstract: Biological mass spectrometry was employed to investigate the identification of various collagen types and their degradation processes during the tail degeneration ofXenopus laevistadpole metamorphosis development. Tail samples were collected at NF 61－65. The collagen types were identified using high-performance liquid chromatography coupled with tandem mass spectrometer (HPLC-MS), and quantitatively analyzed based on marker peptides. Mass spectrometry analysis revealed the presence of collagen types Ⅰ, Ⅱ, Ⅲ, Ⅳ, Ⅴ, Ⅵ, and Ⅻ in the enzymatic digestion products ofXenopus laevistail samples. Collagen type Ⅰ marker peptide GVLGPQGAR was chosen as an external standard for quantification to investigate changes in its content during different growth stages. Similarly, dynamic changes in collagen content for types Ⅲ, Ⅵ and Ⅻ were also analyzed using the same method. The results demonstrated that each type of collagen exhibited a faster degradation rate during NF 61－63 stage accompanied by tail degeneration; however, in NF 64－65 stage when tail atrophy and degeneration ceased, the degradation rate slowed down significantly. Furthermore, the study investigated matrix metallo proteinase (MMPs) types present in tail samples at different stages, and preliminarily explored the relationship between dynamic changes in diameter of tail collagen fibers.

Key words: Xenopus laevis, collagen, collagen degradation, marker peptides, HPLC-MS