Characterization of collagen from haddock skin and wound healing properties of its hydrolysates.
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.
College of Marine Life Science, Ocean University of China, 5 Yushan Road, 266003 Qingdao, People's Republic of China.
Qi Feng
QF
Dang
Han
H
Liu
Jing Quan
JQ
Yan
Cheng Sheng
CS
Liu
Ya
Y
Liu
Jing
J
Li
Jing Jing
JJ
Li
D000818:Animals; D001760:Bleeding Time; D001777:Blood Coagulation; D002645:Chickens; D003094:Collagen / Q000737:chemistry*; D005399:Fishes; D006470:Hemorrhage; D006868:Hydrolysis; D008297:Male; D051379:Mice; D008807:Mice, Inbred BALB C; D008970:Molecular Weight; D018919:Neovascularization, Physiologic; D010063:Ovum; D012867:Skin / Q000737:chemistry*; D012995:Solubility; D013053:Spectrophotometry; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature; D014466:Ultraviolet Rays; D014945:Wound Healing
D003094:Collagen