Physicochemical properties of succinylated calfskin pepsin-solubilized collagen.
Some physicochemical properties of calfskin pepsin-solubilized collagen (PSC) and succinylated PSC (SPSC) were compared. The amino acid profile remained significantly unchanged. Sodium dodecylsulphate-polyacrylamide gel electrophoresis showed that subunits of SPSC migrated less than those of PSC. The denaturation temperatures of PSC and SPSC were 38.4 degrees C and 34.7 degrees C respectively. Succinylation slightly altered the triple-helical conformation of collagen, as determined by circular dichroism.
Zhang
Zhongkai
Z
The Key Laboratory of Leather Chemistry and Engineering of the Ministry of Education, Sichuan University, Chengdu, PR China.
Liu
Wentao
W
Li
Dong
D
Li
Guoying
G
D000818:Animals; D002417:Cattle; D003094:Collagen / Q000737:chemistry* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D010434:Pepsin A / Q000378:metabolism; D011487:Protein Conformation; D011489:Protein Denaturation; D012867:Skin / Q000737:chemistry*; D012995:Solubility; D013386:Succinates; D013696:Temperature
D013386:Succinates; D003094:Collagen; D010434:Pepsin A