Collagen,　one　of　the　most　abundant　structural　proteins　found　in　vertebrates,　has　been　extensively　used　for　biomedical　applications.　The　objectives　of　this　study　were　to　isolate　and　characterize　acid-soluble　collagen　(ASC)　from　haddock　(Melanogrammus　aeglefinus)　skins　and　to　investigate　the　biological　function　of　ASC　hydrolysates　in　wound　healing.　Amino　acid　composition,　SDS-PAGE　and　FTIR　suggested　that　the　ASC　is　most　likely　type　I　collagen　with　well-maintained　helical　structures.　Both　the　denaturation　and　shrinkage　temperatures　of　ASC　isolated　from　haddock　skins　were　lower　than　those　of　mammalian　collagens.　The　average　molecular　weights　of　hydrolysates　decreased　with　the　increase　in　HCl　concentration　as　well　as　hydrolysis　times.　ASC　and　hydrolysates　with　more　molecules　(53.8　kDa)　decreased　the　bleeding　and　clotting　times　and　promoted　order　2　vessel　formation　effectively.　All　the　experimental　groups,　including　the　ASC　group　and　its　hydrolysate　groups,　could　accelerate　epithelialization　and　shorten　the　wound　healing　time　of　mice.　The　ASC　from　haddock　skin　could　therefore　serve　as　an　alternative　collagen　for　skin　wound　healing.