Structural property and in vitro self-assembly of shark type I collagen.
The main structure of shark type I collagen is similar to that of land mammals, with a partial difference in amino acid sequence and post-translational modification. By static light scattering, the weight-average molecular weight of shark collagen (7.52 x 10(5)) suggests the presence of some aggregated molecules, oligomeric collagen. The self-assembly curve of shark collagen had a shorter lag phase and a longer growth phase than that of pig collagen. The optimum temperature and pH of shark collagen self-assembly is different from that of pig collagen.
Nomura
Y
Y
Faculty of Agriculture, Tokyo University of Agriculture and Technology, Japan. ny318@cc.tuat.ac.jp
Yamano
M
M
Hayakawa
C
C
Ishii
Y
Y
Shirai
K
K
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003094:Collagen / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism*; D017364:Collagenases / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D012542:Scattering, Radiation; D012754:Sharks / Q000378:metabolism*; D012967:Sodium Dodecyl Sulfate; D012996:Solutions; D013045:Species Specificity; D013552:Swine; D013696:Temperature
D000596:Amino Acids; D012996:Solutions; D012967:Sodium Dodecyl Sulfate; D003094:Collagen; D017364:Collagenases